Loading
PDBj
メニューPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

1BS8

PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER

1BS8 の概要
エントリーDOI10.2210/pdb1bs8/pdb
関連するPDBエントリー1BS4 1BS5 1BS6 1BS7 1BSZ
分子名称PROTEIN (PEPTIDE DEFORMYLASE), PROTEIN (MET-ALA-SER), ZINC ION, ... (5 entities in total)
機能のキーワードhydrolase, iron metalloprotease; protein synthesis
由来する生物種Escherichia coli
詳細
タンパク質・核酸の鎖数6
化学式量合計58989.20
構造登録者
Becker, A.,Schlichting, I.,Kabsch, W.,Groche, D.,Schultz, S.,Wagner, A.F.V. (登録日: 1998-09-01, 公開日: 1999-08-27, 最終更新日: 2023-08-09)
主引用文献Becker, A.,Schlichting, I.,Kabsch, W.,Groche, D.,Schultz, S.,Wagner, A.F.
Iron center, substrate recognition and mechanism of peptide deformylase.
Nat.Struct.Biol., 5:1053-1058, 1998
Cited by
PubMed Abstract: Eubacterial proteins are synthesized with a formyl group at the N-terminus which is hydrolytically removed from the nascent chain by the mononuclear iron enzyme peptide deformylase. Catalytic efficiency strongly depends on the identity of the bound metal. We have determined by X-ray crystallography the Fe2+, Ni2+ and Zn2+ forms of the Escherichia coli enzyme and a structure in complex with the reaction product Met-Ala-Ser. The structure of the complex, with the tripeptide bound at the active site, suggests detailed models for the mechanism of substrate recognition and catalysis. Differences of the protein structures due to the identity of the bound metal are extremely small and account only for the observation that Zn2+ binds more tightly than Fe2+ or Ni2+. The striking loss of catalytic activity of the Zn2+ form could be caused by its reluctance to change between tetrahedral and five-fold metal coordination believed to occur during catalysis. N-terminal formylation and subsequent deformylation
PubMed: 9846875
DOI: 10.1038/4162
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.2 Å)
構造検証レポート
Validation report summary of 1bs8
検証レポート(詳細版)ダウンロードをダウンロード

226707

件を2024-10-30に公開中

PDB statisticsPDBj update infoContact PDBjnumon