1bs7
From Proteopedia
|
PEPTIDE DEFORMYLASE AS NI2+ CONTAINING FORM
Overview
Peptide deformylase is an essential metalloenzyme required for the removal, of the formyl group at the N terminus of nascent polypeptide chains in, eubacteria. The Escherichia coli enzyme uses Fe2+ and nearly retains its, activity on substitution of the metal ion by Ni2+. We have solved the, structure of the Ni2+ enzyme at 1.9-A resolution by x-ray crystallography., Each of the three monomers in the asymmetric unit contains one Ni2+ ion, and, in close proximity, one molecule of polyethylene glycol. Polyethylene, glycol is shown to be a competitive inhibitor with a KI value of 6 mM with, respect to formylmethionine under conditions similar to those used for, crystallization. We have also solved the structure of the inhibitor-free, enzyme at 2.5-A resolution. The two structures are identical within the, estimated errors of the models. The hydrogen bond network stabilizing the, active site involves nearly all conserved amino acid residues and well, defined water molecules, one of which ligates to the tetrahedrally, coordinated Ni2+ ion.
About this Structure
1BS7 is a Single protein structure of sequence from Escherichia coli with SO4 and NI as ligands. Active as Formylmethionine deformylase, with EC number 3.5.1.31 Full crystallographic information is available from OCA.
Reference
Structure of peptide deformylase and identification of the substrate binding site., Becker A, Schlichting I, Kabsch W, Schultz S, Wagner AF, J Biol Chem. 1998 May 8;273(19):11413-6. PMID:9565550
Page seeded by OCA on Tue Nov 20 11:52:37 2007
