1kuh

From Proteopedia

Revision as of 14:32, 18 December 2007

ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS

Overview

A zinc endoprotease produced by Streptomyces caespitosus (ScNP), specifically hydrolyzes the peptide bond at the imino side of aromatic, residues and is the smallest protease found to date. Although ScNP carries, the zinc-binding sequence HEXXH, its primary structure of 132 amino acid, residues differs from those of other known zinc metalloendoproteases., X-ray structural analysis of ScNP at 1.6 A resolution revealed that, despite a lack of sequence homology, the common topological feature of, main-chain folding and a beta-turn containing methionine, which is a, feature of the zinc metalloendoprotease superfamily of metzincins, is, conserved in ScNP. The zinc atom of ScNP is tetrahedrally ligated by the, two histidines in the HEXXH sequence, an aspartate residue and a water, molecule. Thus, ScNP represents a novel subfamily of metzincins with a, HEXXHXXGXXD zinc-binding sequence. A plausible substrate recognition, pocket to which aromatic residues bind is located near the catalytic zinc, ion.

About this Structure

1KUH is a Single protein structure of sequence from Streptomyces caespitosus with ZN and CA as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.

Reference

Structure of the zinc endoprotease from Streptomyces caespitosus., Kurisu G, Kinoshita T, Sugimoto A, Nagara A, Kai Y, Kasai N, Harada S, J Biochem (Tokyo). 1997 Feb;121(2):304-8. PMID:9089404

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