ArticleMolecular microbiology2013
Structure-function analysis of the LytM domain of EnvC, an activator of cell wall remodelling at the Escherichia coli division site.
Article in Molecular microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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Who cites it
49 citing papers in PubMed, 76 citations in OpenAlex.
- Interaction mechanisms of MXene with bacterial division proteins: towards efficient antibacterial materials.Journal of molecular modeling · 2026Article
- Targeting the Disease Response With NlpD and LytM for Effective Nonantibiotic Treatment of Urinary Tract Infections.The Journal of infectious diseases · 2026Article
- Transposon-insertion sequencing reveals NlpD as a vulnerability in intracellular survival and pathogenesis of Salmonella 4,[5],12:i:.PLoS pathogens · 2026Article
- Article
- A new class of type VI secretion system effectors can carry two toxic domains and are recognized through the WHIX motif for export.PLoS biology · 2025Article
- Modulation of the lytic apparatus by the FtsEX complex within the bacterial division machinery.FEBS letters · 2024Review
- Peptidoglycan Endopeptidase PBP7 Facilitates the Recruitment of FtsN to the Divisome and Promotes Peptidoglycan Synthesis in Escherichia coli.Molecular microbiology · 2024Article
- Article
- In Vivo Cross-Linking Sheds Light on the Salmonella Divisome in Which PBP3 and PBP3Molecular microbiology · 2024Article
- Article
- Structure predictions and functional insights into Amidase_3 domain containing N-acetylmuramyl-L-alanine amidases from Deinococcus indicus DR1.BMC microbiology · 2024Article
- NlpI-Prc Proteolytic Complex Mediates Peptidoglycan Synthesis and Degradation via Regulation of Hydrolases and Synthases inInternational journal of molecular sciences · 2023Article
- DipM controls multiple autolysins and mediates a regulatory feedback loop promoting cell constriction in Caulobacter crescentus.Nature communications · 2023Article
- Activator-induced conformational changes regulate division-associated peptidoglycan amidases.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mechanistic insights into the regulation of cell wall hydrolysis by FtsEX and EnvC at the bacterial division site.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Regulation of peptidoglycan hydrolases: localization, abundance, and activity.Current opinion in microbiology · 2023Review
- Metal cofactor stabilization by a partner protein is a widespread strategy employed for amidase activation.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- BB0761, a MepM homolog, contributes to Borrelia burgdorferi cell division and mammalian infectivity.Molecular microbiology · 2022Article
- One fold, many functions-M23 family of peptidoglycan hydrolases.Frontiers in microbiology · 2022Review
- A LytM-Domain Factor, ActS, Functions in Two Distinctive Peptidoglycan Hydrolytic Pathways inFrontiers in microbiology · 2022Article
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Authors and funding
6 authors at 3 institutions in 3 countries.
Funding
Abstract
Proteins with LytM (Peptidase_M23) domains are broadly distributed in bacteria and have been implicated in a variety of important processes, including cell division and cell-shape determination. Most LytM-like proteins that have been structurally and/or biochemically characterized are metallo-endopeptidases that cleave cross-links in the peptidoglycan (PG) cell wall matrix. Notable exceptions are the Escherichia coli cell division proteins EnvC and NlpD. These LytM factors are not hydrolases themselves, but instead serve as activators that stimulate PG cleavage by target enzymes called amidases to promote cell separation. Here we report the structure of the LytM domain from EnvC, the first structure of a LytM factor implicated in the regulation of PG hydrolysis. As expected, the fold is highly similar to that of other LytM proteins. However, consistent with its role as a regulator, the active-site region is degenerate and lacks a catalytic metal ion. Importantly, genetic analysis indicates that residues in and around this degenerate active site are critical for amidase activation in vivo and in vitro. Thus, in the regulatory LytM factors, the apparent substrate binding pocket conserved in active metallo-endopeptidases has been adapted to control PG hydrolysis by another set of enzymes.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.