1KUH

ZINC PROTEASE FROM STREPTOMYCES CAESPITOSUS

1KUH の概要

• エントリーDOI: 10.2210/pdb1kuh/pdb
• 分子名称: ZINC PROTEASE, ZINC ION, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: metalloproteinase, hydrolase
• 由来する生物種: Streptomyces caespitosus
• 細胞内の位置: Secreted: P56406
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14492.81

構造登録者

Kurisu, G.,Kinoshita, T.,Sugimoto, A.,Nagara, A.,Kai, Y.,Kasai, N.,Harada, S. (登録日: 1996-02-22, 公開日: 1997-03-12, 最終更新日: 2024-10-23)

主引用文献

Kurisu, G.,Kinoshita, T.,Sugimoto, A.,Nagara, A.,Kai, Y.,Kasai, N.,Harada, S.
Structure of the zinc endoprotease from Streptomyces caespitosus.
J.Biochem.(Tokyo), 121:304-308, 1997

PubMed Abstract: 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.

PubMed: 9089404

実験手法

X-RAY DIFFRACTION (1.6 Å)