1tuf

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spinqualitylabelsall models 1tuf, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of Diaminopimelate Decarboxylase from m. jannaschi

Overview

Cocrystal structures of Methanococcus jannaschii diaminopimelate, decarboxylase (DAPDC) bound to a substrate analog, azelaic acid, and its, L-lysine product have been determined at 2.6 A and 2.0 A, respectively., This PLP-dependent enzyme is responsible for the final step of L-lysine, biosynthesis in bacteria and plays a role in beta-lactam antibiotic, resistance in Staphylococcus aureus. Substrate specificity derives from, recognition of the L-chiral center of diaminopimelate and a system of, ionic "molecular rulers" that dictate substrate length. A coupled-enzyme, assay system permitted measurement of kinetic parameters for recombinant, DAPDCs and inhibition constants (K(i)) for azelaic acid (89 microM) and, other substrate analogs. Implications for rational design of, broad-spectrum antimicrobial agents targeted against DAPDCs of, drug-resistant strains of bacterial pathogens, such as Staphylococcus, aureus, are discussed.

About this Structure

1TUF is a Single protein structure of sequence from Methanocaldococcus jannaschii with AZ1 as ligand. Active as Diaminopimelate decarboxylase, with EC number 4.1.1.20 Full crystallographic information is available from OCA.

Reference

Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor., Ray SS, Bonanno JB, Rajashankar KR, Pinho MG, He G, De Lencastre H, Tomasz A, Burley SK, Structure. 2002 Nov;10(11):1499-508. PMID:12429091

Page seeded by OCA on Wed Nov 21 03:36:03 2007