December 2007 issue
Cover illustration: Superposition of different binding modes in complex structures of -ketoacyl-ACP-syntase (KAS I) with the ligands thiolactomycin (cyan), cerulenin (gold) and aminothiazole (green) (p. 1208).
The first crystal structures of human dCK in complex with products are reported.
β-Ketoacyl-ACP synthase is a key target for the treatment of infectious diseases. A structure-based biophysical screening approach identified for the first time a synthetic small molecule, 2-phenylamino-4-methyl-5-acetylthiazole, that binds to the active site of the enzyme. Implications for the use of this information in drug discovery are discussed.
Crystal structures of recombinant branched-chain keto acid decarboxylase (KdcA) from L. lactis were determined as a binary complex with the cofactor thiamin diphosphate and as a complex with an analogue of a reaction intermediate to 1.6 and 1.8 Å resolution, respectively.
Familial oncocytic thyroid carcinoma is associated with a missense mutation, P308Q, in the C-terminal domain of Tim44. Here, the crystal structure of the human Tim44 C-terminal domain in complex with pentaethylene glycol at 1.9 Å resolution is reported.
A simple three-parameter ADP model for macromolecules has been devised and examined with respect to its potential use in macromolecular crystallography.
Two structures of regulatory chain mutants Asp19Ar and His20Ar of E. coli aspartate transcabomylase are presented. Small structural changes illustrate small, but significant, changes in kinetic behavior of both mutant enzymes and suggest that His20 and Asp19 participate in heterotropic regulatory pathways.
A 2.1 Å resolution crystal structure of the B. subtilis organic hydroperoxide-resistance protein B reveals details of the stereochemistry of the disulfide bonds in the transient oxidized form of the enzyme.