2Y6I

Crystal Structure of Collagenase G from Clostridium histolyticum in complex with Isoamylphosphonyl-Gly-Pro-Ala at 3.25 Angstrom Resolution

2Y6I の概要

• エントリーDOI: 10.2210/pdb2y6i/pdb
• 関連するPDBエントリー: 2Y3U 2Y50
• 関連するBIRD辞書のPRD_ID: PRD_000989
• 分子名称: COLLAGENASE, ISOAMYLPHOSPHONYL-GLY-PRO-ALA, ZINC ION, ... (8 entities in total)
• 機能のキーワード: hydrolase-inhibitor complex, hydrolase, gluzincin, metalloprotease, hydrolase/inhibitor
• 由来する生物種: CLOSTRIDIUM HISTOLYTICUM; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 90480.77

構造登録者

Eckhard, U.,Brandstetter, H. (登録日: 2011-01-21, 公開日: 2011-09-28, 最終更新日: 2024-10-09)

主引用文献

Eckhard, U.,Schoenauer, E.,Nuess, D.,Brandstetter, H.
Structure of Collagenase G Reveals a Chew-and -Digest Mechanism of Bacterial Collagenolysis
Nat.Struct.Mol.Biol., 18:1109-, 2011

PubMed Abstract: Collagen constitutes one-third of body protein in humans, reflecting its extensive role in health and disease. Of similar importance, therefore, are the idiosyncratic proteases that have evolved for collagen remodeling. The most efficient collagenases are those that enable clostridial bacteria to colonize their host tissues; but despite intense study, the structural and mechanistic basis of these enzymes has remained elusive. Here we present the crystal structure of collagenase G from Clostridium histolyticum at 2.55-Å resolution. By combining the structural data with enzymatic and mutagenesis studies, we derive a conformational two-state model of bacterial collagenolysis, in which recognition and unraveling of collagen microfibrils into triple helices, as well as unwinding of the triple helices, are driven by collagenase opening and closing.

PubMed: 21947205
DOI: 10.1038/NSMB.2127

実験手法

X-RAY DIFFRACTION (3.25 Å)