This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1kuh
From Proteopedia
|
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. ... [(full description)]
About this Structure
1KUH is a [Single protein] structure of sequence from [Streptomyces caespitosus] with ZN and CA as [ligands]. 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
Page seeded by OCA on Mon Oct 29 19:28:39 2007
Categories: Single protein | Streptomyces caespitosus | Harada, S. | Kai, Y. | Kasai, N. | Kinoshita, T. | Kurisu, G. | Nagara, A. | Sugimoto, A. | CA | ZN | Hydrolase | Metalloproteinase
