1BS4

PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL

Summary for 1BS4

• Entry DOI: 10.2210/pdb1bs4/pdb
• Related: 1BS5 1BS6 1BS7 1BS8 1BSZ
• Descriptor: PROTEIN (PEPTIDE DEFORMYLASE), ZINC ION, NONAETHYLENE GLYCOL, ... (5 entities in total)
• Functional Keywords: complex(enzyme-inhibitor), hydrolase, iron metalloprotease, protein synthesis
• Biological source: Escherichia coli
• Total number of polymer chains: 3
• Total formula weight: 59310.56

Authors

Becker, A.,Schlichting, I.,Kabsch, W.,Groche, D.,Schultz, S.,Wagner, A.F.V. (deposition date: 1998-09-01, release date: 1999-08-27, Last modification date: 2023-08-09)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.9 Å)