Ca 2+ ‐induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation-Reference-Cited by-同舟云学术

Ca 2+ ‐induced orientation of tandem collagen binding domains from clostridial collagenase ColG permits two opposing functions of collagen fibril formation and retardation

Published:2018-08-20 Issue:17 Volume:285 Page:3254-3269
ISSN:1742-464X
Container-title:The FEBS Journal
language:en
Short-container-title:FEBS J

Author:

Caviness Perry¹,Bauer Ryan¹,Tanaka Keisuke²,Janowska Katarzyna¹,Roeser Jeffrey Randall¹,Harter Dawn¹,Sanders Jes¹,Ruth Christopher¹,Matsushita Osamu³,Sakon Joshua¹

Affiliation:

1. Department of Chemistry and Biochemistry University of Arkansas Fayetteville AR USA

2. Nippi Research Institute of Biomatrix Toride Ibaraki Japan

3. Department of Bacteriology Graduate School of Medicine, Dentistry and Pharmaceutical Sciences Okayama University Japan

Funder

National Institutes of Health

Arkansas Biosciences Institute

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1111/febs.14611

Reference49 articles.

1. High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils

2. Proposal to restrict the genus Clostridium Prazmowski to Clostridium butyricum and related species

3. Structure of collagenase G reveals a chew-and-digest mechanism of bacterial collagenolysis

4. A bacterial collagen-binding domain with novel calcium-binding motif controls domain orientation

5. A Study of the Collagen-binding Domain of a 116-kDaClostridium histolyticum Collagenase

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