ArticleScientific reports2015
High resolution structure of an M23 peptidase with a substrate analogue.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 75 citations in OpenAlex.
- Heterodimerization of staphylococcal phage φ2638A endolysin isoforms and their functional role in bacterial lysis.microLife · 2025Article
- Article
- Chemical shift assignments of the catalytic domain of Staphylococcus aureus LytM.Biomolecular NMR assignments · 2024Article
- A dynamic bactofilin cytoskeleton cooperates with an M23 endopeptidase to control bacterial morphogenesis.eLife · 2024Article
- Antimicrobial peptidase lysostaphin at subinhibitory concentrations modulates staphylococcal adherence, biofilm formation, and toxin production.BMC microbiology · 2023Article
- Staphylococcus aureus sacculus mediates activities of M23 hydrolases.Nature communications · 2023Article
- Revealing Corynebacterium glutamicum proteoforms through top-down proteomics.Scientific reports · 2023Article
- Genome-Wide Subtraction Analysis and Reverse Vaccinology to Detect Novel Drug Targets and Potential Vaccine Candidates Against Ehrlichia chaffeensis.Applied biochemistry and biotechnology · 2023Article
- Structural and Functional Characterization of β-lytic Protease fromInternational journal of molecular sciences · 2022Article
- Influence of NaCl and pH on lysostaphin catalytic activity, cell binding, and bacteriolytic activity.Applied microbiology and biotechnology · 2022Article
- Electrostatic Interaction with the Bacterial Cell Envelope Tunes the Lytic Activity of Two Novel Peptidoglycan Hydrolases.Microbiology spectrum · 2022Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- Structural Characterization of EnpA D,L-Endopeptidase fromInternational journal of molecular sciences · 2021Article
- The active repertoire of Escherichia coli peptidoglycan amidases varies with physiochemical environment.Molecular microbiology · 2021Article
- Diversification of LytM Protein Functions in Polar Elongation and Cell Division ofFrontiers in microbiology · 2021Article
- Two New M23 Peptidoglycan Hydrolases With Distinct Net Charge.Frontiers in microbiology · 2021Article
- The X-ray crystal structure of the N-terminal domain of Ssr4, a Schizosaccharomyces pombe chromatin-remodelling protein.Acta crystallographica. Section F, Structural biology communications · 2020Article
- MMPphg from the thermophilic Meiothermus bacteriophage MMP17 as a potential antimicrobial agent against both Gram-negative and Gram-positive bacteria.Virology journal · 2020Article
- Roles of LysM and LytM domains in resuscitation-promoting factor (Rpf) activity and Rpf-mediated peptidoglycan cleavage and dormant spore reactivation.The Journal of biological chemistry · 2020Article
- Structural basis of peptidoglycan endopeptidase regulation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
LytM is a Staphylococcus aureus autolysin and a homologue of the S. simulans lysostaphin. Both enzymes are members of M23 metallopeptidase family (MEROPS) comprising primarily bacterial peptidoglycan hydrolases. LytM occurs naturally in a latent form, but can be activated by cleavage of an inhibitory N-terminal proregion. Here, we present a 1.45 Å crystal structure of LytM catalytic domain with a transition state analogue, tetraglycine phosphinate, bound in the active site. In the electron density, the active site of the peptidase, the phosphinate and the "diglycine" fragment on the P1' side of the transition state analogue are very well defined. The density is much poorer or even absent for the P1 side of the ligand. The structure is consistent with the involvement of His260 and/or His291 in the activation of the water nucleophile and suggests a possible catalytic role for Tyr204, which we confirmed by mutagenesis. Possible mechanisms of catalysis and the structural basis of substrate specificity are discussed based on the structure analysis.
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