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1twi
From Proteopedia
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , and | ||||||
| Gene: | LYSA, MJ1097 (Methanocaldococcus jannaschii) | ||||||
| Activity: | Diaminopimelate decarboxylase, with EC number 4.1.1.20 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine
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
1TWI is a Single protein structure of sequence from Methanocaldococcus jannaschii. 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 Sun Mar 23 13:47:44 2008
Categories: Diaminopimelate decarboxylase | Methanocaldococcus jannaschii | Single protein | Bonanno, J B. | Burley, S K. | He, G. | Lencastre, H De. | NYSGXRC, New York Structural GenomiX Research Consortium. | Pinho, M G. | Rajashankar, K R. | Ray, S S. | Tomasz, A. | LYS | MG | PLP | Antibiotic resistance | Lysine biosynthesis | New york structural genomix research consortium | Nysgxrc | Protein structure initiative | Psi | Structural genomic | T135
