issue contents

ISSN: 2053-230X

December 2017 issue

Highlighted illustration

Cover illustration: SAM-dependent methyltransferase from Pyrococcus horikoshii in complex with the cofactor SAM (Pampa et al., p. 706).

research communications

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The crystal structure of dTDP-4-dehydro-β-L-rhamnose reductase (RfbD) from Bacillus anthracis was determined at 2.65 Å resolution in complex with NADP+. RfbD is the fourth enzyme of the dTDP-β-L-rhamnose-biosynthetic pathway and provides evidence that RfbD homologs in Gram-positive bacteria exhibit key differences in the residues important for oligomerization and metal utilization compared with those from many Gram-negative bacteria.

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The crystal structure of a pyridoxal 5′-phosphate-dependent aspartate racemase derived from Scapharca broughtonii has been resolved at 1.90 Å resolution.

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A very low cost method for carrying out imaging of trace fluorescently labeled protein crystallization plates is described.

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The crystal structure of dTDP-6-deoxy-D-xylo-4-hexulose 3,5-epimerase (RfbC) from B. anthracis was determined at 1.63 Å resolution in complex with dTDP and pyrophosphate. RfbC is the third enzyme of the dTDP-L-rhamnose-biosynthetic pathway and only crystallized in the presence of the other three members of the pathway RfbA, RfbB and RfbD.

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The acetoacetate decarboxylase-like superfamily contains a subset of proteins that are predicted to be involved in secondary metabolism based on gene context. Swit_4259, a protein of unknown function, belongs to this emerging family V subset, in which the overall fold resembles prototypical acetoacetate decarboxylases, but the active-site architecture leads to a divergence in function.

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The crystal structure of an anti-idiotype VLR, VLR39, at 1.5 Å resolution is presented and compared with those of other protein-specific VLRs. Binding studies with purified components confirms a VLR39–Fv interaction.

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The crystal structure of a fibronectin type III domain from human collagen α1 type XX (residues Pro386–Pro466) was solved at 2.5 Å resolution.

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The sensor domain of the PscF chemoreceptor from the plant pathogen P. syringae pv. actinidiae has been cloned, expressed, purified and crystallized. Preliminary X-ray diffraction data from native and selenomethionine-labelled protein crystals were collected to 1.46 and 2.46 Å resolution, respectively.

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The crystal structure of SAM-dependent methyltransferase from P. horikoshii in complex with the cofactor SAM was solved by X-ray diffraction. The monomeric structure consists of a Rossmann-like fold (domain I) and a substrate-binding domain (domain II). The cofactor binds at the interface between adjacent subunits.

addenda and errata

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