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. 2022 Oct 21;13:1036964. doi: 10.3389/fmicb.2022.1036964

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Copyright © 2022 Razew, Schwarz, Mitkowski, Sabala and Kaus-Drobek.

This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

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Crystal structures of representative M23 metallopeptidases: LytM (blue; 4ZYB), Lysostaphin (violet; 4QPB), EnpA (magenta; 6SMK), and LasA (green, 3IT5). The M23 peptidases sequence conservation score was calculated in the ConSurf server and is displayed on LytM surface (PDB ID: 4ZYB; Landau et al., 2005). (A) Active sites and loop architectures are represented as cartoons. The active site residues are depicted as bold sticks and labelled accordingly. The zinc ion is shown as a yellow sphere. The LytM was crystallized in the presence of tetraglycine phosphinate, and the resulting complex served as a model for the substrate-binding mechanism. (B) The top view (upper panel) and site-zoomed view (bottom panel) of the corresponding surface represent the M23 structures.