issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

April 2018 issue

Highlighted illustration

Cover illustration: The structure of 2A protease from human rhinovirus C15 (Ling et al., p. 255). The majority of outbreaks of the common cold are caused by human rhinoviruses (HRVs), and the 2A protease of HRVs is known to play an important role in the propagation of the virus and in viral replication. It is hoped that this structure will help in the design of efficient peptide inhibitors or antiviral compounds to block the replication of HRVs.

research communications


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The crystal structure of chorismate mutase from B. phymatum reveals the prototypical AroQγ topology, as observed in the homolog from M. tuberculosis.

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Pyrimidine-nucleoside phosphorylases participate in DNA/RNA synthesis and are essential in anticancer drug therapies. Here, the structure of pyrimidine-nucleoside phosphorylase from B. subtilis in complex with imidazole is reported at 1.88 Å resolution.

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The putative large and small terminase genes of bacteriophage N4 that are essential for genome packaging were identified, cloned and expressed, and the proteins were purified. The purified wild-type large terminase exhibited basal and small terminase-stimulated ATPase activity and produced thin plate-like crystals under one condition.

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This article reports the crystal structure of the apo form and the AMPPNP- and Mn2+- bound forms of the essential helicase of ZIKV refined to 1.78 and 1.3 Å resolution, respectively.

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The crystal structure of proliferating cell nuclear antigen (PCNA) bound to a peptide carrying an AlkB homologue 2 PCNA-interacting motif consensus sequence, RFLVK, was determined. The phenylalanine and leucine residues of the peptide, plus a preceding hydrophobic residue, are involved in interactions with PCNA, providing a structural basis for regulation of the PCNA interaction.

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The 2.2 Å resolution crystal structure of the homologous recombination protein RecR from P. aeruginosa PAO1 is reported. The crystal structure shows that dimeric P. aeruginosa RecR forms a ring-like tetramer architecture via crystal symmetry.

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The putative compatible solute-binding protein ProX from Mycobacterium tuberculosis was found to bind polyphenols instead of betaine, choline or carnitine. X-ray diffraction data were collected to 2.10 Å resolution.

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The crystal structure of glyceraldehyde-3-phosphate dehydrogenase from S. agalactiae is reported at 1.36 Å resolution.

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The crystal structure of methionyl-tRNA synthetase (MetRS) from Mycobacterium tuberculosis in complex with the catalytic intermediate methionyl adenylate at 2.6 Å resolution is described. Comparisons with other MetRSs, including human cytosolic MetRS, reveal substantial differences that could be of use in the development of new antituberculosis inhibitors.

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The 2.6 Å resolution crystal structure of the 2A protease from human rhinovirus C15 (HRV-C15) reveals the presence of a conserved His–Asp–Cys catalytic triad and a Zn2+-binding site. Comparison with the structures of 2A proteases from other enteroviruses reveals that the substrate-binding cleft of the 2A protease from HRV-C15 shows a more open conformation and is presumably more accessible for substrate binding.

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Complexes of the rice immune receptor RGA5A_S and the rice blast fungus effector AVR1-CO39 were prepared using mixing, by fusing the two proteins in one gene construct and by co-expression. Diffracting crystals were obtained using the first two methods under two different conditions.
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