Crystal structure of the folded domains of Xrs2 from Saccharomyces cerevisiae

We present the 2.4 Å resolution X-ray crystal structure of the N-terminal folded domains of S. cerevisiae Xrs2, confirming a tandem FHA–BRCT1–BRCT2 domain architecture similar to that of Schizosaccharomyces pombe Nbs1. Comparative structural analyses and electrostatic surface mapping suggest that the FHA and tandem BRCT domains serve as a key binding site for phosphorylated protein partners.

Crystal structure of the virulence protein J (VirJ) domain 1 from Brucella abortus

Virulence protein J (VirJ) is produced by the bacterial pathogen Brucella abortus and contains two domains, D1 and D2. The crystal structure of VirJ^D1 is presented at a resolution of 1.7 Å and displays an α/β-hydrolase fold with a central β-sheet surrounded by α-helices. Structural comparison with other members of the family suggests that VirJ^D1 lacks the characteristic catalytic triad.

Triosephosphate isomerase from Fasciola hepatica: high-resolution crystal structure as a drug target

The high-resolution crystal structure of triosephosphate isomerase from F. hepatica was solved at 1.51 Å resolution in its monoclinic form, revealing details of the dimer interface critical for enzyme function. Molecular docking with the fasciolocide triclabendazole suggests selective binding near nonconserved residues, highlighting this enzyme as a promising parasite-specific drug target.

Off-target binding of the histone de­acetylase inhibitor vorinostat to carbonic anhydrase II and IX

We determined high-resolution crystal structures of the histone deacetylase inhibitor vorinostat bound to both human carbonic anhydrase II and a carbonic anhydrase IX active-site mimic. Thermal shift assays using differential scanning fluorimetry showed minimal stabilization of either carbonic anhydrase by vorinostat, in contrast to the potent carbonic anhydrase inhibitor acetazolamide.

Crystal structure of a seven-substitution mutant of hydroxynitrile lyase from rubber tree

The crystal structure of HNL6V, a seven-substitution variant of hydroxynitrile lyase from rubber tree, reveals that engineered mutations designed to mimic the homologous esterase SABP2 shift the catalytic atom positions intermediate between those of the parent enzyme and the target esterase.