Structural Investigations on the SH3b Domains of <i>Clostridium perfringens</i> Autolysin through NMR Spectroscopy and Structure Simulation Enlighten the Cell Wall Binding Function

Structural Investigations on the SH3b Domains of <i>Clostridium perfringens</i> Autolysin through NMR Spectroscopy and Structure Simulation Enlighten the Cell Wall Binding Function

<i>Clostridium perfringens</i> autolysin (CpAcp) is a peptidoglycan hydrolase associated with cell separation, division, and growth. It consists of a signal peptide, ten SH3b domains, and a catalytic domain. The structure and function mechanisms of the ten SH3bs related to cell wall pept...

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Bibliographic Details
Main Authors: Yubao Shan, Xiaoling He, Zi Wang, Xiali Yue, Jiang Zhu, Yunhuang Yang, Maili Liu
Format: Article
Language:English
Published: MDPI AG 2021-09-01
Series:Molecules
Subjects:
Acp
SH3b
NMR structure
peptidoglycan hydrolase
cell wall
Online Access:https://www.mdpi.com/1420-3049/26/18/5716

Internet

https://www.mdpi.com/1420-3049/26/18/5716

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