issue contents

Journal logoSTRUCTURAL BIOLOGY
COMMUNICATIONS
ISSN: 2053-230X

November 2021 issue

Highlighted illustration

Cover illustration: Crystal structure of the [2Fe–S] protein I (Shethna protein I) from the model organism for nitrogen fixation Azotobacter vinelandii [Kabasakal et al. (2021), Acta Cryst. F77, 407–411].

editorial


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Editors of Acta Cryst. F Structural Biology Communications discuss their plans for topical reviews.

scientific commentaries


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Measurements of protein dense phases reveal the presence of highly ordered protein nanostructures. Such phases may be candidates for structural biology measurements on next-generation instruments for molecules that are difficult or impossible to crystallize.

topical reviews


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Thirty years of crystal structures of the enzyme hydroxymethylbilane synthase are surveyed in this topical review. These crystal structures aim at the elucidation of the structural basis of the complex reaction mechanism involving the formation of tetrapyrrole from individual porphobilinogen units.

research communications


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Acetylxylan esterase from Caldanaerobacter subterraneus subsp. tengcongensis (TTE0866) catalyzes the deacetylation of cellulose acetate. The crystal structure of TTE0866 at 1.9 Å resolution revealed the catalytic domain, but electron density was not observed for the N-terminal region. The active-site conformation of TTE0866 was similar to those of other carbohydrate esterase family 4 enzymes, but the orientation of the Trp264 side chain was distinct, which may contribute to its reactivity towards highly substituted cellulose acetate.

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Several Azotobacter iron–sulfur proteins probably play roles in the complex redox chemistry that Azotobacter must maintain when fixing nitrogen. The 2.1 Å resolution crystal structure of the [2Fe–2S] protein I (Shethna protein I) from Azotobacter vinelandii reveals a homodimer similar to the structure of the thioredoxin-like [2Fe–2S] protein from Aquifex aeolicus, with the [2Fe–2S] cluster coordinated by the surrounding conserved cysteine residues.

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Microstructural measurements of salted-out protein dense phases show that they contain highly ordered protein nanostructures that assemble hierarchically to create the phase. Such phases may be candidates for structural biology measurements on next-generation instruments for molecules that are difficult or impossible to crystallize in bulk.


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The crystal structure of N-terminal degron-truncated human glutamine synthetase was determined at 2.95 Å resolution, which revealed that the N-degron is not essential for decamer formation. The study also investigated the roles of N-degron in oligomerization and enzymatic activities through biochemical analyses.
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