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

Yan Wang, Peng Wang, Hai-Yan Cao, Hai-Tao Ding, Hai-Nan Su, Shi-Cheng Liu, Guangfeng Liu, Xia Zhang, Chun-Yang Li, Ming Peng, Fuchuan Li, Shengying Li, Yin Chen, Xiu-Lan Chen () and Yu-Zhong Zhang ()
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Yan Wang: Shandong University
Peng Wang: Ocean University of China
Hai-Yan Cao: Shandong University
Hai-Tao Ding: Polar Research Institute of China
Hai-Nan Su: Shandong University
Shi-Cheng Liu: Qingdao Vland Biotech Inc.
Guangfeng Liu: Chinese Academy of Sciences
Xia Zhang: Qingdao Vland Biotech Inc.
Chun-Yang Li: Ocean University of China
Ming Peng: Shandong University
Fuchuan Li: Shandong University
Shengying Li: Shandong University
Yin Chen: Ocean University of China
Xiu-Lan Chen: Shandong University
Yu-Zhong Zhang: Ocean University of China

Nature Communications, 2022, vol. 13, issue 1, 1-14

Abstract: Abstract 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.

Date: 2022
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DOI: 10.1038/s41467-022-28264-1

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