issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

July 2016 issue

Highlighted illustration

Cover illustration: Structure of Alcaligenes faecalis D-3-hydroxybutyrate dehydrogenase in complex with NAD+ and D-3-hydroxybutyrate (Kanazawa et al., p. 507). As a trigger for attacking the bound cofactor, the rocking movement of the small domain is pushing the bound substrate down, through a hydrogen bond. The other complexes with malonate and methylmalonate suggest the inhibition mechanism of the catalytic reaction.

research communications


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Crystal structures of A. faecalis D-3-hydroxybutyrate dehydrogenase in complex with NAD+ and D-3-hydroxybutyrate, malonate or methylmalonate reveal the mechanisms of the catalytic reaction and its inhibition.

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The crystal structure of Cerulean-S175G was compared with those of Cerulean and SCFP3A, which are notable variants of enhanced cyan fluorescent protein (ECFP). A detailed comparison of the three structures revealed that the notable conformational changes of ECFP variants can be understood mainly in terms of the interaction between the Trp66 residue of the chromophore and residues 145–148 of β-strand 7.

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The crystal structure and preliminary structure-based mutagenesis and activity studies of aspartate transcarbamoylase from P. falciparum are reported.

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Thiolases catalyze the Claisen condensation of two acetyl-CoA molecules to give acetoacetyl-CoA, as well as the reverse degradative reaction. The present work reveals various structural aspects of E. coli thiolase, including enzyme kinetics, substrate binding, tetrameric organization and the active-site water network.

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The structure of a double hexamer of the N-terminal domain of the minichromosome maintenance protein from P. furiosus is presented and analyzed.

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A V. cholerae MATE transporter was crystallized using the lipidic cubic phase (LCP) method. X-ray diffraction data sets were collected from single crystals obtained in a sandwich plate and a sitting-drop plate to resolutions of 2.5 and 2.2 Å, respectively.

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The acetate-bound form of copper was found in the crystal structure of the multicopper oxidase CueO. The exogenous acetate ion can reach the copper active site through the water channel in the CueO molecule.

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The crystallization, data collection and experimental phasing using the multiwavelength anomalous dispersion technique of A. thaliana FUT1 is described.

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A subcomplex of the transsulfursome with tRNACys (SepCysS–SepCysE–tRNACys) represents the second reaction step of Cys-tRNACys synthesis in an indirect pathway. Diffraction-quality crystals (2.6 Å resolution) of this complex were obtained. X-ray crystallographic analysis showed that the complex consists of a SepCysS dimer, a SepCysE dimer and one tRNACys.

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Crystals of psCA3 undergo a space-group transition from P21212 to I222 following cryoannealing, resulting in higher resolution diffraction.
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