1BSZ

PEPTIDE DEFORMYLASE AS FE2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL

1BSZ の概要

• エントリーDOI: 10.2210/pdb1bsz/pdb
• 関連するPDBエントリー: 1BS5 1BS6 1BS7 1BS8
• 分子名称: PROTEIN (PEPTIDE DEFORMYLASE), FE (III) ION, NONAETHYLENE GLYCOL, ... (5 entities in total)
• 機能のキーワード: complex(enzyme-inhibitor), hydrolase, iron metalloprotease, protein synthesis
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 59281.87

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: 1999-08-26, 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

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

実験手法

X-RAY DIFFRACTION (1.9 Å)