Acta Crystallographica Section D

Biological Crystallography

Volume 68, Part 2 (February 2012)



[Issue Author Index][Volume Author Index]
[Cover illustration] Cover illustration: A surface representation of two adjacent linear diubiquitin molecules in two views related by a 90° rotation around the horizontal axis (p. 102). The distal ubiquitins are denoted in darker orange, whereas the proximal moieties are shown in tan. The hydrophobic patches (Leu8, Ile44 and Val70) are shown in red and are aligned on the same side in every other moiety along the straight line of linear diubiquitin chains in the crystal.

research papers


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Acta Cryst. (2012). D68, 95-101  [ doi:10.1107/S0907444911051031 ]

Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly

C. Dong, H.-F. Hou, X. Yang, Y.-Q. Shen and Y.-H. Dong

Synopsis: BamD is part of the Escherichia coli outer membrane protein complex (BAM complex) and is essential for the survival of E. coli. The structure of BamD at 2.6 Å resolution shows that this lipoprotein is composed of ten [alpha]-helices that form five tetratricopeptide-repeat (TPR) motifs.

PDB reference: 3q5m

Online 6 January 2012


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Acta Cryst. (2012). D68, 102-108  [ doi:10.1107/S0907444911051195 ]

Structure of a compact conformation of linear diubiquitin

A. Rohaim, M. Kawasaki, R. Kato, I. Dikic and S. Wakatsuki

Synopsis: A new crystal structure of linear diubiquitin adopts a compact conformation that differs from its previously reported extended conformation.

PDB reference: 3axc

Online 13 January 2012


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Acta Cryst. (2012). D68, 109-116  [ doi:10.1107/S090744491105133X ]

Four complete turns of a curved 310-helix at atomic resolution: the crystal structure of the peptaibol trichovirin I-4A in a polar environment suggests a transition to [alpha]-helix for membrane function

R. Gessmann, D. Axford, R. L. Owen, H. Brückner and K. Petratos

Synopsis: The first structure of a subfamily 4 peptaibol antibiotic, trichovirin I-4A, is described at atomic resolution. The structure suggests a conformational transition to obtain the necessary amphiphilicity for membrane insertion and water/ion transport across the hydrophobic barrier.

PDB reference: 3sbn

Online 6 January 2012


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Acta Cryst. (2012). D68, 117-123  [ doi:10.1107/S0907444911051626 ]

Structural basis of the strict phospholipid binding specificity of the pleckstrin homology domain of human evectin-2

S. Okazaki, R. Kato, Y. Uchida, T. Taguchi, H. Arai and S. Wakatsuki

Synopsis: The 1.75 Å resolution X-ray crystallographic structure of human evectin-2 pleckstrin homology domain revealed ligand-induced conformational change. This structural change effectively explains the strict phospholipid binding specificity.

PDB reference: 3via

Online 13 January 2012


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Acta Cryst. (2012). D68, 124-133  [ doi:10.1107/S0907444911052085 ]

Global radiation damage at 300 and 260 K with dose rates approaching 1 MGy s-1

M. Warkentin, R. Badeau, J. B. Hopkins, A. M. Mulichak, L. J. Keefe and R. E. Thorne

Synopsis: Approximately half of global radiation damage to thaumatin crystals can be outrun at 260 K if data are collected in less than 1 s.

Online 17 January 2012


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Acta Cryst. (2012). D68, 134-143  [ doi:10.1107/S0907444911052231 ]

Structural studies on Mycobacterium tuberculosis DXR in complex with the antibiotic FR-900098

C. Björkelid, T. Bergfors, T. Unge, S. L. Mowbray and T. A. Jones

Synopsis: The structure of M. tuberculosis DXR (also known as IspC) in complex with the antibiotic FR-900098, NADPH and manganese was determined. This new crystal form diffracts to the highest resolution (1.65 Å) reported to date for this enzyme from any species.

PDB reference: 4a03

Online 6 January 2012


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Acta Cryst. (2012). D68, 144-153  [ doi:10.1107/S0907444911052632 ]

Covalent modifications of the catalytic tyrosine in octahaem cytochrome c nitrite reductase and their effect on the enzyme activity

A. A. Trofimov, K. M. Polyakov, T. V. Tikhonova, A. V. Tikhonov, T. N. Safonova, K. M. Boyko, P. V. Dorovatovskii and V. Popov

Synopsis: An unusual covalent bond between the side chains of the catalytic Tyr residue and Gln decreases the activity of cytochrome c nitrite reductase. The Tyr residue is a proton donor during the catalysis.

PDB references: 3rkh, 3sce, 3lgq, 3lg1, 3s7w and 3uu9

Online 13 January 2012


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Acta Cryst. (2012). D68, 154-159  [ doi:10.1107/S0907444911053042 ]

Structural insights into human Kif7, a kinesin involved in Hedgehog signalling

M. Klejnot and F. Kozielski

Synopsis: The human Kif7 motor domain structure provides insights into a kinesin of medical significance.

PDB references: 4a14 and 2xt3

Online 13 January 2012


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Acta Cryst. (2012). D68, 160-168  [ doi:10.1107/S0907444911053157 ]

Structures of NodZ [alpha]1,6-fucosyltransferase in complex with GDP and GDP-fucose

K. Brzezinski, Z. Dauter and M. Jaskolski

Synopsis: Crystal structures of the bacterial [alpha]1,6-fucosyltransferase NodZ in complex with GDP and GDP-fucose are presented.

PDB references: 3siw and 3six

Online 6 January 2012


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Acta Cryst. (2012). D68, 169-175  [ doi:10.1107/S0907444911053327 ]

Structure of an RNA/DNA dodecamer corresponding to the HIV-1 polypurine tract at 1.6 Å resolution

P. Drozdzal, K. Michalska, R. Kierzek, L. Lomozik and M. Jaskolski

Synopsis: The high-resolution crystal structure of an RNA/DNA dodecamer with the HIV-1 polypurine-tract sequence reveals an A-type hybrid duplex with a complete absence of any C2'-endo ribonucleotides and with segments of increased flexibility along the RNA chain.

PDB reference: 3ssf

Online 6 January 2012


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Acta Cryst. (2012). D68, 176-185  [ doi:10.1107/S090744491105414X ]

Structure of the effector-binding domain of the arabinose repressor AraR from Bacillus subtilis

K. Procházková, K. Cermáková, P. Pachl, I. Sieglová, M. Fábry, Z. Otwinowski and P. Rezácová

Synopsis: The crystal structure of the effector-binding domain of the transcriptional repressor AraR from B. subtilis in complex with the effector molecule (L-arabinose) was determined at 2.2 Å resolution. A detailed analysis of the crystal identified a dimer organization that is distinctive from that of other members of the GalR/LacI family.

PDB reference: 3tb6

Online 17 January 2012


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Acta Cryst. (2012). D68, 186-193  [ doi:10.1107/S0907444911054503 ]

The role of Asp116 in the reductive cleavage of dioxygen to water in CotA laccase: assistance during the proton-transfer mechanism

C. S. Silva, J. M. Damas, Z. Chen, V. Brissos, L. O. Martins, C. M. Soares, P. F. Lindley and I. Bento

Synopsis: The role of Asp116 in the pronotation events taking place during CotA laccase catalytic mechanism was investigated. The crystal structure determination of three distinct mutants (D116A, D116N and D116E), produced by site-saturation mutagenesis, together with theoretical calculations have provided evidence of its importance during the reductive cleavage of dioxygen to water.

PDB references: 4a66, 4a67 and 4a68

Online 17 January 2012


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Acta Cryst. (2012). D68, 194-199  [ doi:10.1107/S0907444911042430 ]

Notes for authors 2012

Online 17 January 2012


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