1kuh
From Proteopedia
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'''ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS''' | '''ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS''' | ||
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[[Category: Nagara, A.]] | [[Category: Nagara, A.]] | ||
[[Category: Sugimoto, A.]] | [[Category: Sugimoto, A.]] | ||
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Revision as of 20:10, 2 May 2008
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. 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. 1997 Feb;121(2):304-8. PMID:9089404 Page seeded by OCA on Fri May 2 23:10:57 2008
