One fold, many functions—M23 family of peptidoglycan hydrolases
Abstract
Bacterial cell walls are the guards of cell integrity. They are composed of peptidoglycan that provides rigidity to sustain internal turgor and ensures isolation from the external environment. In addition, they harbor the enzymatic machinery to secure cell wall modulations needed throughout the bacterial lifespan. The main players in this process are peptidoglycan hydrolases, a large group of enzymes with diverse specificities and different mechanisms of action. They are commonly, but not exclusively, found in prokaryotes. Although in most cases, these enzymes share the same molecular function, namely peptidoglycan hydrolysis, they are leveraged to perform a variety of physiological roles. A well-investigated family of peptidoglycan hydrolases is M23 peptidases, which display a very conserved fold, but their spectrum of lytic action is broad and includes both Gram- positive and Gram- negative bacteria. In this review, we summarize the structural, biochemical, and functional studies concerning the M23 family of peptidases based on literature and complement this knowledge by performing large-scale analyses of available protein sequences. This review has led us to gain new insight into the role of surface charge in the activity of this group of enzymes. We present relevant conclusions drawn from the analysis of available structures and indicatemore »
- Authors:
- Publication Date:
- Sponsoring Org.:
- USDOE Office of Electricity (OE), Advanced Grid Research & Development. Power Systems Engineering Research
- OSTI Identifier:
- 1894151
- Grant/Contract Number:
- NOR/POLNOR/PrevEco/0021/2019
- Resource Type:
- Published Article
- Journal Name:
- Frontiers in Microbiology
- Additional Journal Information:
- Journal Name: Frontiers in Microbiology Journal Volume: 13; Journal ID: ISSN 1664-302X
- Publisher:
- Frontiers Media SA
- Country of Publication:
- Switzerland
- Language:
- English
Citation Formats
Razew, Alicja, Schwarz, Jan-Niklas, Mitkowski, Paweł, Sabala, Izabela, and Kaus-Drobek, Magdalena. One fold, many functions—M23 family of peptidoglycan hydrolases. Switzerland: N. p., 2022.
Web. doi:10.3389/fmicb.2022.1036964.
Razew, Alicja, Schwarz, Jan-Niklas, Mitkowski, Paweł, Sabala, Izabela, & Kaus-Drobek, Magdalena. One fold, many functions—M23 family of peptidoglycan hydrolases. Switzerland. https://doi.org/10.3389/fmicb.2022.1036964
Razew, Alicja, Schwarz, Jan-Niklas, Mitkowski, Paweł, Sabala, Izabela, and Kaus-Drobek, Magdalena. Fri .
"One fold, many functions—M23 family of peptidoglycan hydrolases". Switzerland. https://doi.org/10.3389/fmicb.2022.1036964.
@article{osti_1894151,
title = {One fold, many functions—M23 family of peptidoglycan hydrolases},
author = {Razew, Alicja and Schwarz, Jan-Niklas and Mitkowski, Paweł and Sabala, Izabela and Kaus-Drobek, Magdalena},
abstractNote = {Bacterial cell walls are the guards of cell integrity. They are composed of peptidoglycan that provides rigidity to sustain internal turgor and ensures isolation from the external environment. In addition, they harbor the enzymatic machinery to secure cell wall modulations needed throughout the bacterial lifespan. The main players in this process are peptidoglycan hydrolases, a large group of enzymes with diverse specificities and different mechanisms of action. They are commonly, but not exclusively, found in prokaryotes. Although in most cases, these enzymes share the same molecular function, namely peptidoglycan hydrolysis, they are leveraged to perform a variety of physiological roles. A well-investigated family of peptidoglycan hydrolases is M23 peptidases, which display a very conserved fold, but their spectrum of lytic action is broad and includes both Gram- positive and Gram- negative bacteria. In this review, we summarize the structural, biochemical, and functional studies concerning the M23 family of peptidases based on literature and complement this knowledge by performing large-scale analyses of available protein sequences. This review has led us to gain new insight into the role of surface charge in the activity of this group of enzymes. We present relevant conclusions drawn from the analysis of available structures and indicate the main structural features that play a crucial role in specificity determination and mechanisms of latency. Our work systematizes the knowledge of the M23 family enzymes in the context of their unique antimicrobial potential against drug-resistant pathogens and presents possibilities to modulate and engineer their features to develop perfect antibacterial weapons.},
doi = {10.3389/fmicb.2022.1036964},
journal = {Frontiers in Microbiology},
number = ,
volume = 13,
place = {Switzerland},
year = {Fri Oct 21 00:00:00 EDT 2022},
month = {Fri Oct 21 00:00:00 EDT 2022}
}
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