issue contents

Journal logoSTRUCTURAL
ISSN: 2059-7983

August 2017 issue

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Cover illustration: Combatting antibiotic resistance. The role of conserved surface hydrophobic residues in the carbapenemase activity of the class D [beta]-lactamases (Smith et al., p. 692).

topical reviews

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This paper reviews the recent advances in computational template-based structural modelling and proposes the subclustering of protein domain superfamilies to guide the template-selection process.

research papers

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The nucleoprotein of Toscana virus forms mainly open fivefold oligomers consistent with the encapsidation mechanism of phlebovirus RNA both in solution and under physiological conditions.

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Hydroxycitrate was co-crystallized with the amino-terminal portion of human ATP-citrate lyase in order to learn how this competitive inhibitor binds. Crystals diffracting to high resolution were obtained by adding cleavage sites in the protein to remove a disordered linker. This strategy could be useful for other proteins that do not crystallize well.

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An in-depth analysis of the PEG-bound C-terminal SH3 domain of myosin IB from Entamoeba histolytica has been performed, which reveals the mode of ligand recognition and will be helpful in the identification of probable binding partners of E. histolytica myosin IB.

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The structure of CheR1 in complex with c-di-GMP-bound MapZ is reported and the complex biochemical process which involves CheR1, MapZ, SAH/SAM and c-di-GMP is revealed.

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The crystal structure of the class D carbapenemase OXA-143 from A. baumannii shows that a conserved valine residue on the protein surface controls access of the deacylating water molecule to the active site of the enzyme. Analysis of the structures of other class D carbapenemases implicates movement of juxtaposed surface valine and leucine residues in a universal deacylation mechanism for these enzymes.

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