1TWI
Crystal structure of Diaminopimelate Decarboxylase from m. jannaschii in co-complex with L-lysine
1TWI の概要
| エントリーDOI | 10.2210/pdb1twi/pdb |
| 関連するPDBエントリー | 1TUF |
| 分子名称 | Diaminopimelate decarboxylase, PYRIDOXAL-5'-PHOSPHATE, MAGNESIUM ION, ... (5 entities in total) |
| 機能のキーワード | antibiotic resistance, diaminopimelate 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 | 4 |
| 化学式量合計 | 195663.78 |
| 構造登録者 | Rajashankar, K.R.,Ray, S.S.,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: 2004-07-01, 公開日: 2004-07-27, 最終更新日: 2023-08-23) |
| 主引用文献 | Rajashankar, K.R.,Ray, S.S.,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 Cited by 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: 12429091DOI: 10.1016/S0969-2126(02)00880-8 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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