1bs4
From Proteopedia
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PEPTIDE DEFORMYLASE AS ZN2+ CONTAINING FORM (NATIVE) IN COMPLEX WITH INHIBITOR POLYETHYLENE GLYCOL
Overview
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 ... [(full description)]
About this Structure
1BS4 is a [Single protein] structure of sequence from [Escherichia coli] with SO4, ZN and 2PE as [ligands]. Active as [[1]], with EC number [3.5.1.31]. Full crystallographic information is available from [OCA].
Reference
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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