forthcoming articles in Acta Crystallographica Section D

The following articles are a selection of those recently accepted for publication in Acta Crystallographica Section D: Biological Crystallography.

See also Forthcoming articles in all IUCr journals.

Na⁺/K⁺ exchange switches the catalytic apparatus of K-dependent plant L-asparaginase

M. Bejger, B. Imiolczyk, D. Clavel, M. Gilski, A. Pajak, F. Marsolais and M. Jaskolski

Synopsis: Three crystal structures of potassium-dependent plant L-asparaginase were solved in complexes with K⁺, Na⁺, and both cations. A novel alkali metal binding loop Val111-Ser118 (the activation loop) changes its conformation upon K⁺/Na⁺ exchange, leading to a reconfiguration of three key residues, His117, Arg224, Glu250 (the catalytic switch), to allow or prevent substrate binding in the active site of the enzyme.

Automated Identification of Crystallographic Ligands using Sparse Density Representations

C. G. Carolan and V. S. Lamzin

Synopsis: A novel procedure for identifying ligands in macromolecular crystallographic electron density maps is introduced. Density clusters in such maps can be rapidly attributed to one of 82 different ligands in an automated manner.

The structure of a deoxygenated 400 kDa hemoglobin reveals ternary and quaternary structural changes of giant hemoglobins

N. Numoto, T. Nakagawa, R. Ohara, T. Hasegawa, A. Kita, T. Yoshida, T. Maruyama, K. Imai, Y. Fukumori and K. Miki

Synopsis: The first structure of the deoxygenated form of 400 kDa hemoglobin from a tube worm Lamellibrachia satsuma is reported.

Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole

P. Asztalos, A. Müller, W. Hölke, H. Sobek and M. G. Rudolph

Synopsis: Crystal structures of Lysobacter enzymogenes wild-type LysC and of the K30R variant near the substrate binding site have been determined in complex with the covalent inhibitor TLCK that mimics a tetrahedral reaction intermediate. Hydrogen atom density indicates a hydroxyl group in the "oxyanion" hole.

Structural and functional characterization of human and murine C5a anaphylatoxins

J. A. Schatz-Jakobsen, L. Yatime, C. Larsen, S. V. Petersen, A. Klos and G. R. Andersen

Synopsis: The structure of the human C5aR antagonist, C5a-A8, reveals a three-helix bundle conformation similar to the one observed for human C5a-desArg, whereas murine C5a and C5a-desArg both form the canonical four-helix bundle. These conformational differences are discussed in light of the differential C5aR activation properties observed for the human and murine complement anaphylatoxins accross species.

Bacterial Periplasmic Sialic Acid Binding Proteins Exhibit a Conserved Binding Site

T. Gangi Setty, C. Cho, S. Govindappa, M. A. Apicella and S. Ramaswamy

Synopsis: Structure-function studies of sialic acid binding proteins from Fusobacterium nucleatum, Pasteurella multocida, Vibrio cholera and Haemophilus influenzae reveals a conserved network of hydrogen bonds involved in conformational change on ligand binding.

Structural and Bioinformatic Characterization of an Acinetobacter baumannii Type II Carrier Protein

C. L. Allen and A. M. Gulick

Structure of LCMV Nucleoprotein Provides a Template for Understanding Arenavirus Replication and Immunosuppression

B. R. West, K. M. Hastie and E. O. Saphire

Synopsis: The crystal structure of the Lymphocytic Choriomeningitis Virus NP C-terminal domain adopts the fold of an exonuclease and provides an important structural template for the study of this prototypic arenavirus.

L-allo-Threonine aldolase with H128Y/S292R mutation from Aeromonas jandaei DK-39 reveals the structural basis of changes in substrate stereoselectivity

H.-M. Qin, F. L. Imai, T. Miyakawa, M. Kataoka, N. Kitamura, N. Urano, K. Mori, H. Kawabata, M. Okai, J. Ohtsuka, F. Hou, K. Nagata, S. Shimizu and M. Tanokura

Synopsis: The crystal structures of Aeromonas jandaei LATA and its mutant were refined to 2.59 and 2.50 Å resolutions, respectively. The structural basis of the substrate specificity and stereoselectivity has been elucidated.

Structure solution of DNA binding proteins and complexes with ARCIMBOLDO libraries

K. Pröpper, K. Meindl, M. Sammito, B. Dittrich, G. M. Sheldrick, E. Pohl and I. Usón

Synopsis: Structure solution of DNA-binding protein structures and complexes, based on the combination of location of DNA-binding protein motif fragments with density modification in a multi solution frame.

Structure of BamA, an Essential Factor of Outer Membrane Protein Biogenesis

R. Albrecht, M. Schütz, P. Oberhettinger, M. Faulstich, I. Bermejo, T. Rudel, K. Diederichs and K. Zeth

Synopsis: The cloning, purification and crystallization of the E. coli BamA -barrel domain including one POTRA domain is reported. The crystal structure allows detailed insights into the mechanism of outer membrane protein biogenesis in Gram-negative bacteria.

Structural Elucidation of Hormonal Inhibition Mechanism of the Bile Acid Cholate on Human Carbonic Anhydrase II

C. D. Boone, C. Tu and R. McKenna

Synopsis: The structure of human carbonic anhydrase II in complex with cholate has been determined to 1.54 Å resolution. The elucidation of cholate's novel inhibition mechanism will aid in the development of non-sulfur containing, isoform-specific therapeutic agent.

Crystal structures of inactive CRP species reveal the atomic details of allosteric transition that discriminates cyclic nucleotide second messengers

S.-H. Seok, H. Im, H.-S. Won, M.-D. Seo, Y.-S. Lee, H.-J. Yoon, M.-J. Cha, J.-Y. Park and B.-J. Lee

Synopsis: Binding of cAMP and cGMP to the global transcription factor, CRP, results in different allosteric transition of the protein. The cGMP binding induced an inhibitory conformational change of CRP.

Structure of the oligogalacturonate-specific KdgM porin

C. A. J. Hutter, R. Lehner, C. Wirth, G. Condemine, C. Peneff and T. Schirmer

Engineering the internal cavity of neuroglobin demonstrates the role of the heme sliding mechanism

G. Avella, C. Ardiccioni, A. Scaglione, T. Moschetti, C. Rondinelli, L. C. Montemiglio, C. Savino, A. Giuffrè, M. Brunori and B. Vallone

Synopsis: Mutants have been produced that reduce the volume of murine neuroglobin large internal cavity. Their structural and functional characterization sheds light on the role of the cavity itself and of the structural transitions of the heme upon binding.

Structural insights into the mechanism of calmodulin binding to death receptors

P. Cao, W. Zhang, W. Gui, Y. Dong, T. Jiang and Y. Gong

Synopsis: This work reports two crystal structures of calmodulin in complexes with the corresponding binding regions of the death receptors p75^NTR and Fas.

Structural basis for glucose tolerance in GH1 -glucosidases

P. O. de Giuseppe, T. A. C. B. Souza, F. H. M. Souza, L. M. Zanphorlin, C. B. Machado, R. J. Ward, J. A. Jorge, R. P. M. Furriel and M. T. Murakami

Synopsis: The crystal structures of the beta-glucosidase from the fungus Humicola insolens provided new insights into the structural determinants for glucose stimulation in -glucosidases.

In and Out the minor groove: Interaction of an AT-rich DNA with the CD27 drug

F. J. Acosta-Reyes, C. Dardonville, H. P. de Koning, M. Natto, J. A. Subirana and J. L. Campos

Synopsis: We present new features for an antiprotozoal DNA minor-groove binding drug, which acts as a cross-linking agent. It also fills the minor groove of DNA completely and prevents the access of proteins. These features are also expected for other minor groove binding drugs, when associated with adequate DNA targets.

Structural features underlying the selective cleavage of a novel exo-type maltose-forming amylase from Pyrococcus sp. ST04

K.-H. Park, J.-H. Jung, S.-G. Park, M.-E. Lee, J. F. Holden, C.-S. Park and E.-J. Woo

Crystal structure of human CRMP-4: correction of intensities for lattice-translocation disorder

R. Ponnusamy, A. A. Lebedev, S. Pahlow and B. Lohkamp

Synopsis: Crystals of human CRMP-4 showed severe lattice-translocation disorder. Intensities were demodulated using the so called lattice alignment method and a new more general method with simplified parameterization, and the structure is presented.

Structural and functional analysis of the human spliceosomal DEAD-box helicase Prp28

S. Möhlmann, R. Mathew, P. Neumann, A. Schmitt, R. Lührmann and R. Ficner

Synopsis: The crystal structure of the helicase domain of the human spliceosomal DEAD-box protein Prp28 was solved by means of SAD. The binding of ADP and ATP by Prp28 was studied biochemically and analysed with regard to the crystal structure.

CrowdPhase: Crowdsourcing the phase problem

J. Jorda, M. R. Sawaya and T. O. Yeates

Synopsis: We introduce the idea of attacking the phase problem by crowdsourcing. Using an interactive, multi-player, web-based system, participants work simultaneously to select phase sets that correspond to better electron density maps in order to solve low resolution phasing problems.

Structure of tomato wound-induced leucine aminopeptidase sheds light on substrate specificity

K. Duprez, M. A. Scranton, L. L. Walling and L. Fan

Synopsis: The crystal structure of the wound-induced leucine aminopeptidase (LAP) of tomato was determined to 2.20 Å resolution by molecular replacement method. Structural analysis and modeling reveal the structural basis of substrate binding.

O⁶-carboxymethylguanine in DNA forms a sequence context dependent wobble base pair structure with thymine

F. Zhang, M. Tsunoda, Y. Kikuchi, O. Wilkinson, C. L. Millington, G. P. Margison, D. M. Williams and A. Takénaka

Synopsis: O⁶-carboxymethylguanine residue identified in DNA of human colon tissue, which has been linked to diets high in red and processed meats, reveals to form a pair with thymine residue in a new high wobble type, in addition to a Watson-Crick type.

The structure of Plasmodium falciparum serine hydroxymethyltransferase reveals a novel redox switch that regulates its activities

P. Chitnumsub, W. Ittarat, A. Jaruwat, K. Noytanom, W. Amornwatcharapong, W. Pornthanakasem, P. Chaiyen, Y. Yuthavong and U. Leartsakulpanich

Synopsis: The crystal structure of P. falciparum SHMT revealed snapshots of an intriguing disulfide/sulfhydryl switch controlling the functional activity.

Ten years of probabilistic estimates of biocrystal solvent content: new insights via nonparametric kernel density estimate

C. X. Weichenberger and B. Rupp

Synopsis: The widely used 2003 Matthews probability calculator predicting the most probable number of molecules in the asymmetric unit as a function of resolution has been updated with 2013 data, and a new parameter-free kernel density estimator has been implemented. Analysis of multiple parameters confirms that solvent content remains the primary and dominating parameter determining the diffraction limit (resolution) of protein crystals.

The first structure of a bacterial diterpene cyclase: CotB2

R. Janke, C. Görner, M. Hirte, T. Brück and B. Loll

Synopsis: The crystal structure of the bacterial diterpence cyclase CotB2 is presented. Mutation of residues with plasticity in the active site leads to altered products.

Structural characterization of the apo form and NADH binary complex of human lactate dehydrogenase

S. Dempster, S. Harper, J. E. Moses and I. Dreveny

Synopsis: A crystal structure of the human lactate dehydrogenase A apo form suitable for ligand soaking and a NADH binary-complex structure are presented.

A point mutation in the [2Fe-2S] cluster binding region of the NAF-1 protein (H114C) dramatically hinders the cluster donor properties

S. Tamir, Y. Eisenberg-Domovich, A. R. Conlan, J. T. Stofleth, C. H. Lipper, M. L. Paddock, R. Mittler, P. A. Jennings, O. Livnah and R. Nechushtai

A complement to the modern crystallographer's toolbox: caged gadolinium complexes with versatile binding modes

M. Stelter, R. Molina, S. Jeudy, R. Kahn, C. Abergel and J. A. Hermoso

Synopsis: A set of seven caged gadolinium complexes were shown to be excellent compounds for introducing anomalous scatterers into protein crystals for de novo anomalous phasing. Their high phasing power and versatile binding modes make them highly suitable as a heavy-atom screen.

Exploiting fast detectors to enter a new dimension in room-temperature crystallography

R. L. Owen, N. Paterson, D. Axford, J. Aishima, C. Schulze-Briese, J. Ren, E. E. Fry, D. I. Stuart and G. Evans

Synopsis: A departure from a linear or an exponential decay in the diffracting power of macromolecular crystals is observed and accounted for through consideration of a multi-state sequential model.

Diamonds in the rough: a strong case for the inclusion of weak-intensity X-ray diffraction data

J. Wang and R. A. Wing

Structure of the phosphotransferase domain of the bifunctional aminoglycoside-resistance enzyme AAC(6')-Ie-APH(2'')-Ia

C. A. Smith, M. Toth, M. Bhattacharya, H. Frase and S. B. Vakulenko

Synopsis: The crystal structure of the C-terminal phosphotransferase domain of the bifunctional aminoglycoside acetyltransferase-phosphotransferase AAC(6')-Ie-APH(2'')-Ia has been determined to 2.3 Å resolution. The enzyme was crystallized as the Mg₂GDP binary complex.

Structure and mechanism of a nonhaem-iron SAM-dependent C-methyltransferase and its engineering to a hydratase and an O-methyltransferase

X.-W. Zou, Y.-C. Liu, N.-S. Hsu, C.-J. Huang, S.-Y. Lyu, H.-C. Chan, C.-Y. Chang, H.-W. Yeh, K.-H. Lin, C.-J. Wu, M.-D. Tsai and T.-L. Li

Structure of the unique SEFIR domain of human interleukin 17 receptor A reveals a composite ligand-binding site containing a conserved -helix for Act1 binding and IL-17 signaling

B. Zhang, C. Liu, W. Qian, Y. Han, X. Li and J. Deng

Crystallographic and kinetic study of riboflavin synthase from Brucella abortus, a chemotherapeutic target with an enhanced intrinsic flexibility

M. I. Serer, H. R. Bonomi, B. G. Guimarães, R. C. Rossi, F. A. Goldbaum and S. Klinke

Synopsis: This work reports crystal structures of trimeric riboflavin synthase from the pathogen B. abortus both as the apo protein and in complex with several ligands of interest. It is shown that ligand binding drives the assembly of the unique active site of the trimer, and these findings are complemented by a detailed kinetic study on this enzyme, in which marked inhibition by substrate and product was observed.

Structure of human Bloom's syndrome helicase in complex with ADP and duplex DNA

M. K. Swan, V. Legris, A. Tanner, P. M. Reaper, S. Vial, R. Bordas, J. R. Pollard, P. A. Charlton, J. M. C. Golec and J. A. Bertrand

Structure determination of human Fas apoptosis inhibitory molecule and identification of the critical residues linking the interdomain interaction to the anti-apoptotic activity

G. Li, L. Qu, S. Ma, Y. Wu, C. Jin and X. Zheng

The structure of a class 3 nonsymbiotic plant haemoglobin from Arabidopsis thaliana reveals a novel N-terminal helical extension

B. J. Reeder and M. A. Hough

Synopsis: The first crystal structure of a class 3 nonsymbiotic plant haemoglobin is reported to 1.77 Å resolution. The structure revealed a novel N-terminal helical extension that participates extensively in the dimeric interface.

In cellulo structure determination of a novel cypovirus polyhedrin

D. Axford, X. Ji, D. I. Stuart and G. Sutton

Synopsis: The crystal structure of a previously unsolved type of cypovirus polyhedrin has been determined from data collected directly from frozen live insect cells.

The structure of a novel electron-transfer ferredoxin from Rhodopseudomonas palustris HaA2 which contains a histidine residue in its iron-sulfur cluster-binding motif

T. Zhang, A. Zhang, S. G. Bell, L.-L. Wong and W. Zhou

Phosphates in the Z-DNA dodecamer are flexible, but their P-SAD signal is sufficient for structure solution

Z. Luo, M. Dauter and Z. Dauter

Synopsis: An ultrahigh-resolution structure of the Z-DNA dodecamer, solved from the anomalous signal of P atoms, reveals substantial flexibility of the backbone phosphate groups.

Structure of the epimerization domain of tyrocidine synthetase A

S. A. Samel, P. Czodrowski and L.-O. Essen

Synopsis: The synthesis of nonribosomal peptides often introduces D-configured amino acids into the final products. The first crystal structure of the epimerization domain of a nonribosomal peptide synthetase reveals a bilobal architecture and implies a general acid-base mechanism for the LD isomerization of aminoacyl substrates.

Structure of the nisin leader peptidase NisP revealing a C-terminal autocleavage activity

Y. Xu, X. Li, R. Li, S. Li, H. Ni, H. Wang, H. Xu, W. Zhou, P. E. J. Saris, W. Yang, M. Qiao and Z. Rao

Insights into the binding specificity and catalytic mechanism of N-acetylhexosamine 1-phosphate kinases through multiple reaction complexes

K.-C. Wang, S.-Y. Lyu, Y.-C. Liu, C.-Y. Chang, C.-J. Wu and T.-L. Li

Structural analysis and insight into metal-ion activation of the iron-dependent regulator from Thermoplasma acidophilum

H. K. Yeo, Y. W. Park and J. Y. Lee

Synopsis: The crystal structure of T. acidophilum IdeR is reported.

Fingerprinting redox and ligand states in haemprotein crystal structures using resonance Raman spectroscopy

D. Kekilli, F. S. N. Dworkowski, G. Pompidor, M. R. Fuchs, C. R. Andrew, S. Antonyuk, R. W. Strange, R. R. Eady, S. S. Hasnain and M. A. Hough

Flexible torsion-angle noncrystallographic symmetry restraints for improved macromolecular structure refinement

J. J. Headd, N. Echols, P. V. Afonine, N. W. Moriarty, R. J. Gildea and P. D. Adams

Synopsis: Flexible torsion angle-based NCS restraints have been implemented in phenix.refine, allowing improved model refinement at all resolutions. Rotamer correction and rotamer consistency checks between NCS-related amino-acid side chains further improve the final model quality.

An arginine tetrad as mediator of input-dependent and input-independent ATPases in the clock protein KaiC

R. Pattanayek, Y. Xu, A. Lamichhane, C. H. Johnson and M. Egli

Structure of a three-dimensional domain-swapped dimer of the Helicobacter pylori type IV secretion system pilus protein CagL

S. Barden, B. Schomburg, J. Conradi, S. Backert, N. Sewald and H. H. Niemann

Synopsis: CagL mediates contact of the pathogen H. pylori with host-cell integrins. A domain-swapped structure of CagL shows the RGD motif to act as a hinge region embedded in a helix and reveals the structure of the functionally important C-terminus.

Structural basis of sialidase in complex with geranylated flavonoids as potent natural inhibitors

Y. Lee, Y. B. Ryu, H.-S. Youn, J. K. Cho, Y. M. Kim, J.-Y. Park, W. S. Lee, K. H. Park and S. H. Eom

Synopsis: The crystal structure of sialidase from C. perfringens, a pathogenic bacterium causing various gastrointestinal diseases, was determined in complex with a potent natural polyphenolic geranylated flavonoid-based inhibitor. The complex structure and comparative kinetic studies revealed that the geranyl group and C3' hydroxyl group of the flavonoid backbone contribute to inhibition of the bacterial sialidase and generation of the stable enzyme-inhibitor complex.

Structure of the ubiquitin-activating enzyme loaded with two ubiquitin molecules

A. Schäfer, M. Kuhn and H. Schindelin

Synopsis: The structure of a ternary complex consisting of the ubiquitin-activating enzyme Uba1 and two differently bound ubiquitin molecules has been determined by X-ray crystallography. For the first time, the formation of the ubiquitin-acyladenylate could be structurally visualized together with the attachment of a second ubiquitin covalently linked to the active-site cysteine of Uba1. Model-building studies provide insights into the recruitment of ubiquitin-conjugating enzymes.

A novel -xylosidase structure from Geobacillus thermoglucosidasius: the first crystal structure of a glycoside hydrolase family GH52 enzyme reveals unpredicted similarity to other glycoside hydrolase folds

G. Espina, K. Eley, G. Pompidor, T. R. Schneider, S. J. Crennell and M. J. Danson

Synopsis: The first structure of a CAZy glycoside hydrolase family 52 enzyme, that of G. thermoglucosidasius -xylosidase, reveals structural similarities to other families with which it shares less than 13% sequence identity. The substrate-bound complex confirms the active-site residues and is consistent with a retaining mechanism.

Structure of sulfamidase provides insight into the molecular pathology of mucopolysaccharidosis IIIA

N. S. Sidhu, K. Schreiber, K. Pröpper, S. Becker, I. Usón, G. M. Sheldrick, J. Gärtner, R. Krätzner and R. Steinfeld

Synopsis: Mucopolysaccharidosis IIIA is a fatal neurodegenerative disease that typically manifests itself in childhood and is caused by mutations in the gene for the lysosomal enzyme sulfamidase. The first structure of this enzyme is presented, which provides insight into the molecular basis of disease-causing mutations, and the enzymatic mechanism is proposed.

Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker

A. Seul, J. J. Müller, D. Andres, E. Stettner, U. Heinemann and R. Seckler

Synopsis: A single mutation in the linker region renders intact P22 tailspike crystallizable, allowing analysis of the crystal structure of the complete tailspike at high resolution. The mutant protein is still functional, but has to be distorted to fit into a published cryo-EM map, and the structure suggests an important role of the highly conserved linker in intramolecular signal transmission.

Divalent metal ion-based catalytic mechanism of the Nudix hydrolase Orf153 (YmfB) from Escherichia coli

M.-K. Hong, A. J. M. Ribeiro, J.-K. Kim, P.-T.H. Ngo, J. Kim, C. H. Lee, Y.-J. Ahn, P. A. Fernandes, Q. Li, M. J. Ramos and L.-W. Kang

Structural insight into glucose dehydrogenase from the thermoacidophilic archaeon Thermoplasma volcanium

Y. Kanoh, S. Uehara, H. Iwata, K. Yoneda, T. Ohshima and H. Sakuraba

Synopsis: The structure of a medium-chain dehydrogenase reductase-type glucose dehydrogenase showing narrow substrate specificity was determined, and the unique structural features of the enzyme were compared with those of a glucose dehydrogenase showing broad substrate specificity.

Sunitinib: from charge-density studies to interaction with proteins

M. Malinska, K. N. Jarzembska, A. M. Goral, A. Kutner, K. Wozniak and P. M. Dominiak

Coiled-coil deformations in crystal structures: the Measles virus phosphoprotein multimerization domain as an illustrative example

D. Blocquel, J. Habchi, E. Durand, M. Sevajol, F. Ferron, J. Erales, N. Papageorgiou and S. Longhi

Accurate macromolecular crystallographic refinement: incorporation of the linear scaling, semiempirical quantum-mechanics program DivCon into the PHENIX refinement package

O. Y. Borbulevych, J. A. Plumley, R. M. Martin, K. M. Merz and L. M. Westerhoff

Synopsis: Semiempirical quantum-chemical X-ray macromolecular refinement using the program DivCon integrated with PHENIX is described.

IR laser-induced protein crystal transformation

R. Kiefersauer, B. Grandl, S. Krapp and R. Huber

Synopsis: A novel method and the associated instrumentation for improving crystalline order (higher resolution of X-ray diffraction and reduced mosaicity) of protein crystals by precisely controlled heating is demonstrated. Crystal transformation is optically controlled by a video system.

An improved integration method in serial femtosecond crystallography

K. Qu, L. Zhou and Y.-H. Dong

Synopsis: Please provide a synposis (of not more than two sentences) to appear in the Contents listing of the journal.

Structural basis of a novel activity of bacterial 6-pyruvoyltetrahydropterin synthase homologues distinct from mammalian 6-pyruvoyltetrahydro­pterin synthase activity

K. H. Seo, N. N. Zhuang, Y. S. Park, K. H. Park and K. H. Lee

Synopsis: Crystal structures show how bacterial PTPS homologues possess an unusual activity that differs from that of mammalian PTPS enzymes.

A conformational landscape for alginate secretion across the outer membrane of Pseudomonas aeruginosa

J. Tan, S. L. Rouse, D. Li, V. E. Pye, L. Vogeley, A. R. Brinth, J. C. Whitney, P. L. Howell, M. S. P. Sansom and M. Caffrey

Synopsis: Crystal structures of the -barrel porin AlgE reveal a mechanism whereby alginate is exported from P. aeruginosa for biofilm formation.

A slow-forming isopeptide bond in the structure of the major pilin SpaD from Corynebacterium diphtheriae has implications for pilus assembly

H. J. Kang, N. G. Paterson, C. U. Kim, M. Middleditch, C. Chang, H. Ton-That and E. N. Baker

Synopsis: Two crystal structures of the major pilin SpaD from C. diphtheriae have been determined at 1.87 and 2.5 Å resolution. The N-terminal domain is found to contain an isopeptide bond that forms slowly over time in the recombinant protein. Given its structural context, this provides insight into the relationship between internal isopeptide-bond formation and pilus assembly.

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