March 2009 issue
The structures of the two alternatively spliced isoforms of human ketohexokinase, hepatic KHK-C and peripheral KHK-A, and of the ternary complex of KHK-A with the substrate fructose and AMP-PNP have been solved. The differences between KHK-A and KHK-C resulting from the spliced region are subtle and affect thermostability and probably flexibility; the mutations causing fructosuria were modelled.
The structure of the DUF55 domain of human thymocyte nuclear protein 1, which was determined from partially tetartohedrally twinned crystals, is reported.
The structure of the lysosomal 66.3 kDa protein, which crystallizes in the monoclinic space group C2, was solved by means of sulfur SAD phasing using data with an Ranom/Rp.i.m. ratio of 1.1.
The structure of SoxS has been solved in oxidized and reduced forms at 2.1 and 1.9 Å resolution, respectively.
The crystal structures of DAPK–ADP–Mg2+ and DAPK–AMP-PNP–Mg2+ complexes were determined at 1.85 and 2.00 Å resolution, respectively. Comparison of the two nucleotide-bound states with apo DAPK revealed localized changes in the glycine-rich loop region that were indicative of a transition from a more open state to a more closed state on binding of the nucleotide substrate and to an intermediate state with the bound nucleotide product.
Structure of the G225P/G226P mutant of mouse 3(17)α-hydroxysteroid dehydrogenase (AKR1C21) ternary complex is reported at 2.1 Å resolution.
The crystal structure of C2b has been determined at 1.8 Å resolution, which reveals the arrangement of its three complement control protein (CCP) modules. A model for complement component C2 is presented and its conformational changes during the C3-convertase formation are also discussed.
The crystal structure of M. tuberculosis GlmU has been determined in an unliganded form and in complex with UDP-GlcNAc or GlcN-1-P. NMR-based enzymatic activity assays suggest that the presence of acetyl-coenzyme A has an inhibitory effect on uridyltransferase activity.
The structure of uncomplexed plasmepsin II from P. falciparum is shown to contain noncoplanar catalytic aspartic acid residues.