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. 2023 Aug 24;12(9):1362. doi: 10.3390/antibiotics12091362

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© 2023 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).

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Structural and organizational representation of PBPs that play a crucial role in the final stages of peptidoglycan synthesis in S. aureus. The crystal structures of PBP1 (5TRO), PBP2 (2OLU), PBP2a (1VQQ), PBP3 (3VSK), and PBP4 (6C39) are shown. Endogenous PBP1-4 and acquired PBP2a all have a TPase domain, while PBP2 is unique in also possessing a TGase domain. After flipping to the outer side of the cytoplasmic membrane by MurJ, the peptidoglycan precursor Lipid II-Gly5 can be polymerized by the TGase activity of PBP2, and the glycan strands are then cross-linked by the TPase activity of the PBPs [65].