1TUF

Crystal structure of Diaminopimelate Decarboxylase from m. jannaschi

1TUF の概要

• エントリーDOI: 10.2210/pdb1tuf/pdb
• 分子名称: Diaminopimelate decarboxylase, AZELAIC ACID (3 entities in total)
• 機能のキーワード: antibiotic resistance, diamnopimilate decarboxylase, lysine biosynthesis, structural genomics, nysgxrc, t135, psi, protein structure initiative, new york sgx research center for structural genomics, lyase
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 97748.50

構造登録者

Rajashankar, K.,Ray, S.R.,Bonanno, J.B.,Pinho, M.G.,He, G.,De Lencastre, H.,Tomasz, A.,Burley, S.K.,New York SGX Research Center for Structural Genomics (NYSGXRC) (登録日: 2004-06-24, 公開日: 2004-07-20, 最終更新日: 2024-04-03)

主引用文献

Rajashankar, K.,Ray, S.R.,Bonanno, J.B.,Pinho, M.G.,He, G.,De Lencastre, H.,Tomasz, A.,Burley, S.K.
Cocrystal structures of diaminopimelate decarboxylase: mechanism, evolution, and inhibition of an antibiotic resistance accessory factor
Structure, 10:1499-1508, 2002

PubMed Abstract: 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.

PubMed: 12429091
DOI: 10.1016/S0969-2126(02)00880-8

実験手法

X-RAY DIFFRACTION (2.4 Å)