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Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis

The collagenases of Vibrio species, many of which are pathogens, have been regarded as an important virulence factor. However, there is little information on the structure and collagenolytic mechanism of Vibrio collagenase. Here, we report the crystal structure of the collagenase module (CM) of Vibr...

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Autores principales: Wang, Yan, Wang, Peng, Cao, Hai-Yan, Ding, Hai-Tao, Su, Hai-Nan, Liu, Shi-Cheng, Liu, Guangfeng, Zhang, Xia, Li, Chun-Yang, Peng, Ming, Li, Fuchuan, Li, Shengying, Chen, Yin, Chen, Xiu-Lan, Zhang, Yu-Zhong
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2022
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8799719/
https://www.ncbi.nlm.nih.gov/pubmed/35091565
http://dx.doi.org/10.1038/s41467-022-28264-1
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author Wang, Yan
Wang, Peng
Cao, Hai-Yan
Ding, Hai-Tao
Su, Hai-Nan
Liu, Shi-Cheng
Liu, Guangfeng
Zhang, Xia
Li, Chun-Yang
Peng, Ming
Li, Fuchuan
Li, Shengying
Chen, Yin
Chen, Xiu-Lan
Zhang, Yu-Zhong
author_facet Wang, Yan
Wang, Peng
Cao, Hai-Yan
Ding, Hai-Tao
Su, Hai-Nan
Liu, Shi-Cheng
Liu, Guangfeng
Zhang, Xia
Li, Chun-Yang
Peng, Ming
Li, Fuchuan
Li, Shengying
Chen, Yin
Chen, Xiu-Lan
Zhang, Yu-Zhong
author_sort Wang, Yan
collection PubMed
description The collagenases of Vibrio species, many of which are pathogens, have been regarded as an important virulence factor. However, there is little information on the structure and collagenolytic mechanism of Vibrio collagenase. Here, we report the crystal structure of the collagenase module (CM) of Vibrio collagenase VhaC and the conformation of VhaC in solution. Structural and biochemical analyses and molecular dynamics studies reveal that triple-helical collagen is initially recognized by the activator domain, followed by subsequent cleavage by the peptidase domain along with the closing movement of CM. This is different from the peptidolytic mode or the proposed collagenolysis of Clostridium collagenase. We propose a model for the integrated collagenolytic mechanism of VhaC, integrating the functions of VhaC accessory domains and its collagen degradation pattern. This study provides insight into the mechanism of bacterial collagenolysis and helps in structure-based drug design targeting of the Vibrio collagenase.
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spelling pubmed-87997192022-02-07 Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis Wang, Yan Wang, Peng Cao, Hai-Yan Ding, Hai-Tao Su, Hai-Nan Liu, Shi-Cheng Liu, Guangfeng Zhang, Xia Li, Chun-Yang Peng, Ming Li, Fuchuan Li, Shengying Chen, Yin Chen, Xiu-Lan Zhang, Yu-Zhong Nat Commun Article The collagenases of Vibrio species, many of which are pathogens, have been regarded as an important virulence factor. However, there is little information on the structure and collagenolytic mechanism of Vibrio collagenase. Here, we report the crystal structure of the collagenase module (CM) of Vibrio collagenase VhaC and the conformation of VhaC in solution. Structural and biochemical analyses and molecular dynamics studies reveal that triple-helical collagen is initially recognized by the activator domain, followed by subsequent cleavage by the peptidase domain along with the closing movement of CM. This is different from the peptidolytic mode or the proposed collagenolysis of Clostridium collagenase. We propose a model for the integrated collagenolytic mechanism of VhaC, integrating the functions of VhaC accessory domains and its collagen degradation pattern. This study provides insight into the mechanism of bacterial collagenolysis and helps in structure-based drug design targeting of the Vibrio collagenase. Nature Publishing Group UK 2022-01-28 /pmc/articles/PMC8799719/ /pubmed/35091565 http://dx.doi.org/10.1038/s41467-022-28264-1 Text en © The Author(s) 2022 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Wang, Yan
Wang, Peng
Cao, Hai-Yan
Ding, Hai-Tao
Su, Hai-Nan
Liu, Shi-Cheng
Liu, Guangfeng
Zhang, Xia
Li, Chun-Yang
Peng, Ming
Li, Fuchuan
Li, Shengying
Chen, Yin
Chen, Xiu-Lan
Zhang, Yu-Zhong
Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis
title Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis
title_full Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis
title_fullStr Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis
title_full_unstemmed Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis
title_short Structure of Vibrio collagenase VhaC provides insight into the mechanism of bacterial collagenolysis
title_sort structure of vibrio collagenase vhac provides insight into the mechanism of bacterial collagenolysis
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8799719/
https://www.ncbi.nlm.nih.gov/pubmed/35091565
http://dx.doi.org/10.1038/s41467-022-28264-1
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