issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

April 2019 issue

Highlighted illustration

Cover illustration: Phosphoribulokinase (PRK) from Synechococcus sp. strain PCC 6301 [Wilson et al. (2019), Acta Cryst. F75, 278-289]. PRK catalyses the ATP-dependent phosphorylation of ribulose 5-phosphate to give ribulose 1,5-bisphosphate and regulation of this reaction in response to light controls carbon fixation during photosynthesis. Here, the crystal structure of PRK shows that the enzyme is dimeric and has an [alpha]/[beta]-fold with an 18-stranded [beta]-sheet at its core. Interestingly, a disulfide bond is found between Cys40 and the P-loop residue Cys18, revealing the structural basis for the redox inactivation of PRK activity. A second disulfide bond appears to rigidify the dimer interface and may thereby contribute to regulation by the adaptor protein CP12 and glyceraldehyde-3-phosphate dehydrogenase.

research communications


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The structure of a complex of Mycobacterium tuberculosis decaprenyl diphosphate synthase with geranyl S-thiodiphosphate and isopentenyl S-thiodiphosphate was refined to 1.55 Å resolution. It not only shows the magnesium-coordinated configuration for catalysis but also suggests a pathway for product translocation as well as a direction for inhibitor design.

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The structure of a homodimeric, iron-containing alcohol dehydrogenase from a thermophile that utilizes NADP as its coenzyme was solved in three crystal forms. In two crystals one subunit of the asymmetric unit was occupied by NADP and the other was not, while in the third crystal no NADP or iron was present. The coenzyme is encapsulated in a tunnel that penetrates through the molecule, and the iron is totally sequestered.

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The structure of a lipopolysaccharide transport protein B (LptB) is reported. Comparisons with LptBs from different bacterial species reveal that the dimeric assembly is independent of interaction with the rest of the transport machinery and that significant sequence and structural conservation occurs where LptB interacts with its physiological partners.

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The crystal structure of the protein phosphatase PTP-2 from Cydia pomonella granulovirus, a betabaculovirus, has been determined at 1.65 Å resolution. The structure shows that the molecule has a typical protein phosphatase fold with a unique β-sheet extension at the C-terminus.

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The production of nonglycosylated human furin ectodomain via the BacMam expression system is reported. The protein is equally active compared with the glycosylated protein and is readily crystallized; X-ray diffraction was used to solve a high-resolution structure.

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CdOppA and CdAppA are putative extracellular peptide-binding proteins serving cognate ABC transporters in Clostridium difficile. Using purified proteins, no evidence was found for (i) peptide binding to either protein in Thermofluor experiments or (ii) the presence of peptides in the crystal structure of CdAppA. Further sequence analysis suggests that CdOppA is a nickel-transporter protein and that CdAppA may be involved in the transport of a restricted set of peptides.

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A method to obtain improved crystals of the human tetraspanin protein CD9 by protein modification is described.

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The perdeuteration, large crystal growth and neutron diffraction data collection of an E65Q variant of Leishmania mexicana triose-phosphate isomerase are described.

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Homologous expression of the membrane-bound esterase PA2949 from Pseudomonas aeruginosa PA01 and the purification of detergent-solubilized enzyme resulted in stable PA2949 protein that crystallized. The crystals obtained were used for X-ray analysis and diffracted to a resolution of 2.74 Å.

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The crystal structure of phosphoribulokinase from the cyanobacterium Synechococcus sp. PCC 6301 is presented at 2.4 Å resolution. A disulfide bond is found between Cys40 and the P-loop residue Cys18, revealing the structural basis for the redox inactivation of the enzyme. A second disulfide bond appears to rigidify the dimer interface.

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The structure of S-adenosylmethionine synthetase, an essential enzyme from the infectious parasite Cryptosporidium parvum, has been determined. This enzyme form has a less extensive subunit interface than some previously determined structures, and contains key structural differences from the human enzyme in an allosteric site, presenting an opportunity for the design of selective inhibitors against the AdoMet synthetase from this organism.

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The adenylation enzyme IdnL7, which is involved in the biosynthesis of incednine, has been biochemically and structurally characterized. Biochemical analysis showed that IdnL7 selects and activates several small amino acids. The structure of IdnL7 in complex with an L-alanyl-adenylate intermediate mimic explains the broad substrate specificity of IdnL7 towards small L-amino acids.

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Igni18 from Ignicoccus hospitalis was identified to belong to the α/β-hydrolase superfamily and was cloned, purified and crystallized. The crystal belonged to space group R32 and contained one monomer in the asymmetric unit.

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The crystal structure of Ba0331, a putative polysaccharide deacetylase from Bacillus anthracis, was determined. The structure comprises two domains: a fibronectin type 3-like domain and a NodB catalytic domain.
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