1def
From Proteopedia
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[[Category: zinc metalloprotease]] | [[Category: zinc metalloprotease]] | ||
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Revision as of 12:56, 30 October 2007
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PEPTIDE DEFORMYLASE CATALYTIC CORE (RESIDUES 1-147), NMR, 9 STRUCTURES
Overview
Escherichia coli peptide deformylase, a member of the zinc, metalloproteases family, is made up of an active core domain composed of, 147 residues and of an additional and dispensable C-terminal tail of 21, residues. The three-dimensional structure of the catalytic core could be, studied by NMR. 1H and 15N NMR resonances assignments were obtained by, two-dimensional and three-dimensional heteronuclear spectroscopy. The, structure could be calculated using a set of 1015 restraints for the 147, residues of the enzyme. The overall structure is composed of a series of, antiparallel beta-strands which surround two perpendicular alpha-helices., The C-terminal helix contains the HEXXH motif, which is crucial for, activity. This helical arrangement and the way the histidines bind the, zinc ion ... [(full description)]
About this Structure
1DEF is a [Single protein] structure of sequence from [Escherichia coli] with ZN as [ligand]. Active as [Formylmethionine deformylase], with EC number [3.5.1.31]. Structure known Active Site: CAT. Full crystallographic information is available from [OCA].
Reference
A new subclass of the zinc metalloproteases superfamily revealed by the solution structure of peptide deformylase., Meinnel T, Blanquet S, Dardel F, J Mol Biol. 1996 Sep 27;262(3):375-86. PMID:8845003
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