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.

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.

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.

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.