9LYI

Cryo-EM structure of collagenase H (E416Q mutant) from Hathewaya histolytica in complex with collagen model peptide (Pro-Hyp-Gly)12

9LYI の概要

• エントリーDOI: 10.2210/pdb9lyi/pdb
• EMDBエントリー: 63511
• 分子名称: Collagenase ColH, (Pro-Hyp-Gly)12, CALCIUM ION, ... (5 entities in total)
• 機能のキーワード: collagenase, hathewaya histolytica, clostridium histolyticum, metal binding protein
• 由来する生物種: Hathewaya histolytica; 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 122126.91

構造登録者

Oki, H.,Kawahara, K. (登録日: 2025-02-20, 公開日: 2026-04-15)

主引用文献

Oki, H.,Takebe, K.,Bonsu, A.,Fujii, K.,Masuda, R.,Henderson, N.,Mima, T.,Koide, T.,Moradi, M.,Matsushita, O.,Sakon, J.,Kawahara, K.
Bacterial collagenase harnesses collagen geometry for processive cleavage.
Nat Commun, 2026

PubMed Abstract: Collagen, the major structural protein in the animal extracellular matrix, forms a triple helix that resists proteolysis and requires specialised enzymes for degradation. Flesh-eating bacteria secrete collagenases that unwind the collagen triple helix and processively trim Gly-X-Y triplet repeats, yet the molecular basis of this process has remained obscure. Here, cryo-electron microscopy reveals how Hathewaya histolytica collagenase ColH engages its substrate and exploits the helix's architecture for catalysis. ColH encircles a single collagen triple helix in a closed-ring conformation and, through dynamic domain motions, dehydrates and destabilises it. The enzyme undergoes substrate-assisted twisting to adopt a rigid ratcheted conformation, in which one chain is bent into a tripeptide-long 'bight' and threaded into the active site for cleavage, while two uncut strands are partitioned to non-catalytic sites. Release of the bight appears to reset the enzyme, with the uncut strands serving as guiding tracks. Repeated cycling between dynamic and rigid states likely enables triplet-by-triplet translocation, allowing ColH to harness collagen's geometry for processive degradation. These findings reveal a bacterial strategy for collagen unwinding and cleavage distinct from that of mammalian collagenases, highlighting divergent evolutionary solutions for degrading one of nature's most intractable substrates.

PubMed: 41927550
DOI: 10.1038/s41467-026-71099-3

実験手法

ELECTRON MICROSCOPY (2.8 Å)