2BB7
Mn Form Of E. coli Methionine Aminopeptidase In Complex With a quinolinyl sulfonamide inhibitor
2BB7 の概要
エントリーDOI | 10.2210/pdb2bb7/pdb |
分子名称 | Methionine aminopeptidase, MANGANESE (II) ION, SODIUM ION, ... (5 entities in total) |
機能のキーワード | trimetallic, mn(ii)-form, hydrolase, enzyme-inhibitor complex, metalloenzyme |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 29780.91 |
構造登録者 | |
主引用文献 | Huang, M.,Xie, S.X.,Ma, Z.Q.,Hanzlik, R.P.,Ye, Q.Z. Metal mediated inhibition of methionine aminopeptidase by quinolinyl sulfonamides Biochem.Biophys.Res.Commun., 339:506-513, 2006 Cited by PubMed Abstract: Quinolinyl sulfonamides, such as N-(quinolin-8-yl)methanesulfonamide (10) and N-(5-chloroquinolin-8-yl)methanesulfonamide (11), were identified as potent methionine aminopeptidase (MetAP) inhibitors by high throughput screening of a diverse chemical library of small organic compounds. They showed different inhibitory potencies on Co(II)-, Ni(II)-, Fe(II)-, Mn(II)-, and Zn(II)-forms of Escherichia coli MetAP, and their inhibition is dependent on metal concentration. X-ray structures of E. coli MetAP complexed with 10 revealed that the inhibitor forms a metal complex with the residue H79 at the enzyme active site; the complex is further stabilized by an extended H-bond and metal interaction network. Analysis of the inhibition of MetAP by these inhibitors indicates that this is a typical mechanism of inhibition for many non-peptidic MetAP inhibitors and emphasizes the importance of defining in vitro conditions for identifying and evaluating MetAP inhibitors that will be capable of giving information relevant to the in vivo situation. PubMed: 16300729DOI: 10.1016/j.bbrc.2005.11.042 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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