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1JIW

Crystal structure of the APR-APRin complex

1JIW の概要
エントリーDOI10.2210/pdb1jiw/pdb
関連するPDBエントリー1SMP
分子名称ALKALINE METALLOPROTEINASE, PROTEINASE INHIBITOR, ZINC ION, ... (5 entities in total)
機能のキーワードpseudomonas aeruginosa alkaline protease inhibitor, hydrolase-hydrolase inhibitor complex, hydrolase/hydrolase inhibitor
由来する生物種Pseudomonas aeruginosa
詳細
細胞内の位置Secreted: Q03023
Periplasm: Q03026
タンパク質・核酸の鎖数2
化学式量合計61314.28
構造登録者
Hege, T.,Feltzer, R.E.,Gray, R.D.,Baumann, U. (登録日: 2001-07-03, 公開日: 2001-08-15, 最終更新日: 2024-11-20)
主引用文献Hege, T.,Feltzer, R.E.,Gray, R.D.,Baumann, U.
Crystal structure of a complex between Pseudomonas aeruginosa alkaline protease and its cognate inhibitor: inhibition by a zinc-NH2 coordinative bond
J.Biol.Chem., 276:35087-35092, 2001
Cited by
PubMed Abstract: Serralysins are a family of metalloproteases secreted by Gram-negative bacteria into the medium in the form of inactive zymogens. Usually, all serralysin secretors have on the same operon a gene coding for a periplasmic 10-kDa protein, which is an inhibitor of the secreted protease. The recent characterization of the inhibitor of the alkaline protease from Pseudomonas aeruginosa revealed a surprisingly low dissociation constant of 4 pm, contrary to earlier studies on homologous systems, where inhibition constants in the microm range were reported. To approach a more accurate understanding, the crystal structure of the complex between inhibitor and protease from P. aeruginosa was determined at 1.74 A resolution and refined to R(free) = 0.204. The structure reported here shows clearly that the N terminus of the inhibitor forms a coordinative bond to the catalytic Zn(2+) ion with a nitrogen-zinc distance of 2.17 A. We conclude that this interaction adds substantially to the complex stability and show also that similar interactions are found in other metzincin-inhibitor complexes.
PubMed: 11445573
DOI: 10.1074/jbc.M104020200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.74 Å)
構造検証レポート
Validation report summary of 1jiw
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-01-28に公開中

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