issue contents

ISSN: 2053-230X

October 2022 issue

Highlighted illustration

Cover illustration: 1.52 Å structure of the Monkeypox virus profilin-like protein A42R [Minasov et al. (2022), Acta Cryst. F78, 371–377]. Structural comparison of A42R with known members of the profilin family reveals critical differences that support prior biochemical findings that A42R only weakly binds actin and does not bind poly(L-proline).

research communications

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The crystal structure of the Rho-associated coiled-coil kinase 2 (ROCK2) inhibitor belumosudil bound to CK2α suggests ways in which specificity for either ROCK2 or CK2α can be increased.

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PorX is an essential response regulator of the type IX secretion system associated with bacterial pathogenicity, gliding motility and metabolic enzyme secretion. Here, the purification, crystallization and X-ray analysis of PorX from different bacterial species are reported, representing a milestone in the structure–function studies of this essential protein.

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The mutation of a glutamate residue that is conserved among ATP-citrate lyases (ACLYs) and succinyl-CoA synthetases allowed capture of the catalytic intermediate succinyl-phosphate in a high-resolution crystal structure of succinyl-CoA synthetase. This structure clarifies the enzymatic mechanism of ACLY and supports the conclusion that the amino-terminal portion of ACLY catalyzes the formation of citryl-CoA, while the carboxy-terminal portion catalyzes its cleavage into oxaloacetate and acetyl-CoA.

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The structure of the Monkeypox virus protein A42R has been determined at a resolution of 1.52 Å. This protein has a backbone structure similar to that of cellular profilin, but structural variation in loop regions and a surface basic patch support biochemical data showing that this protein has distinct binding interactions with actin and phosphatidylinositol lipids and is not likely to bind proline-rich domain proteins or microtubules.
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