issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

August 2021 issue

Highlighted illustration

Cover illustration: Crystal structure of the TLDc domain of human nuclear receptor coactivator 7 (NCOA7-AS), which acts as an interferon-induced antiviral inhibitor [Arnaud-Arnould et al. (2021), Acta Cryst. F77, 230–237].

research communications


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The crystal structure of the TLDc domain of the human NCOA7-AS protein, which acts as an interferon-induced antiviral inhibitor, is reported.

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Ligilactobacillus ruminis is a strict anaerobic gut bacterium that produces sortase-dependent pili (LrpCBA) consisting of the tip LrpC (∼123 kDa), basal LrpB (∼39 kDa) and backbone LrpA (∼49 kDa) pilin subunits. Here, the strategy used for the recombinant expression, crystallization and X-ray diffraction analysis of all three pilus constituents is reported.

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A structure of the Rhodococcus equi virulence factor VapB in a new crystal form reveals conformational changes in loop regions at the top of the eight-stranded β-barrel. The resulting cavity might form the binding site for a potential ligand.


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233 chemical fragments were screened for binding to the ATPase domain of the Hsp70-x chaperone from the malaria parasite Plasmodium falciparum. Crystallographic structures of this domain in complex with different fragments revealed a major binding site proximal to the ATPase catalytic pocket. It is shown that a residue near this binding site is not conserved between P. falciparum and human erythrocytic Hsp70 chaperones, which may provide a basis for specific inhibition of the parasite enzyme.

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The L-threonine dehydrogenase from Clostridium difficile has been cloned, expressed and crystallized, allowing the X-ray structure to be determined at 2.6 Å resolution with an R factor of 20.0% and an Rfree of 23.9%.
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