1bs8
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PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM IN COMPLEX WITH TRIPEPTIDE MET-ALA-SER
OverviewOverview
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
About this StructureAbout this Structure
1BS8 is a Single protein structure of sequence from Escherichia coli with and as ligands. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Full crystallographic information is available from OCA.
ReferenceReference
Iron center, substrate recognition and mechanism of peptide deformylase., Becker A, Schlichting I, Kabsch W, Groche D, Schultz S, Wagner AF, Nat Struct Biol. 1998 Dec;5(12):1053-8. PMID:9846875
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