Bacterial collagen-binding domain targets undertwisted regions of collagen

Sagaya Theresa Leena Philominathan, Takaki Koide, Osamu Matsushita, Joshua Sakon

研究成果: Article査読

16 被引用数 (Scopus)

抄録

Clostridium histolyticum collagenase causes extensive degradation of collagen in connective tissue that results in gas gangrene. The C-terminal collagen-binding domain (CBD) of these enzymes is the minimal segment required to bind to a collagen fibril. CBD binds unidirectionally to the undertwisted C-terminus of triple helical collagen. Here, we examine whether CBD could also target undertwisted regions even in the middle of the triple helix. Collageneous peptides with an additional undertwisted region were synthesized by introducing a Gly → Ala substitution [(POG)xPOA(POG)y] 3, where x + y = 9 and x > 3). 1H-15N heteronuclear single quantum coherence nuclear magnetic resonance (HSQC NMR) titration studies with 15N-labeled CBD demonstrated that the minicollagen binds to a 10 Å wide 25 Å long cleft. Six collagenous peptides each labeled with a nitroxide radical were then titrated with 15N-labeled CBD. CBD binds to either the Gly → Ala substitution site or to the C-terminus of each minicollagen. Small-angle X-ray scattering measurements revealed that CBD prefers to bind the Gly → Ala site to the C-terminus. The HSQC NMR spectra of 15N-labeled minicollagen and minicollagen with undertwisted regions were unaffected by the titration of unlabeled CBD. The results imply that CBD binds to the undertwisted region of the minicollagen but does not actively unwind the triple helix.

本文言語English
ページ(範囲)1554-1565
ページ数12
ジャーナルProtein Science
21
10
DOI
出版ステータスPublished - 2012 10

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

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