ArticleJournal of molecular biology2014
Structures of a bifunctional cell wall hydrolase CwlT containing a novel bacterial lysozyme and an NlpC/P60 DL-endopeptidase.
Article in Journal of molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Biochemical characterization and X-ray structural and mutagenic analyses of the putative autolysin CdCwlT33800 catalytic domain fromApplied and environmental microbiology · 2025Article
- Peptidoglycan NlpC/P60 peptidases in bacterial physiology and host interactions.Cell chemical biology · 2023Review
- A CRISPR interference screen reveals a role for cell wall teichoic acids in conjugation in Bacillus subtilis.Molecular microbiology · 2022Article
- Biochemical reconstitution defines new functions for membrane-bound glycosidases in assembly of the bacterial cell wall.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cwl0971, a novel peptidoglycan hydrolase, plays pleiotropic roles in Clostridioides difficile R20291.Environmental microbiology · 2021Article
- Article
- Envelope stress responses defend against type six secretion system attacks independently of immunity proteins.Nature microbiology · 2020Article
- Article
- Cell Wall Hydrolases in Bacteria: Insight on the Diversity of Cell Wall Amidases, Glycosidases and Peptidases Toward Peptidoglycan.Frontiers in microbiology · 2019Review
- The cell wall hydrolase Pmp23 is important for assembly and stability of the division ring in Streptococcus pneumoniae.Scientific reports · 2018Article
- Solution scattering study of the Bacillus subtilis PgdS enzyme involved in poly-γ-glutamic acids degradation.PloS one · 2018Article
- Is the LysM domain of L. monocytogenes p60 protein suitable for engineering a protein with high peptidoglycan binding affinity?Bioengineered · 2016Article
- Article
- Structure-guided functional characterization of DUF1460 reveals a highly specific NlpC/P60 amidase family.Structure (London, England : 1993) · 2014Article
- Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans.The FEBS journal · 2014Article
- Resilience of biochemical activity in protein domains in the face of structural divergence.Current opinion in structural biology · 2014Review
- The bifunctional cell wall hydrolase CwlT is needed for conjugation of the integrative and conjugative element ICEBs1 in Bacillus subtilis and B. anthracis.Journal of bacteriology · 2014Article
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11 authors.
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Abstract
Tn916-like conjugative transposons carrying antibiotic resistance genes are found in a diverse range of bacteria. Orf14 within the conjugation module encodes a bifunctional cell wall hydrolase CwlT that consists of an N-terminal bacterial lysozyme domain (N-acetylmuramidase, bLysG) and a C-terminal NlpC/P60 domain (γ-d-glutamyl-l-diamino acid endopeptidase) and is expected to play an important role in the spread of the transposons. We determined the crystal structures of CwlT from two pathogens, Staphylococcus aureus Mu50 (SaCwlT) and Clostridium difficile 630 (CdCwlT). These structures reveal that NlpC/P60 and LysG domains are compact and conserved modules, connected by a short flexible linker. The LysG domain represents a novel family of widely distributed bacterial lysozymes. The overall structure and the active site of bLysG bear significant similarity to other members of the glycoside hydrolase family 23 (GH23), such as the g-type lysozyme (LysG) and Escherichia coli lytic transglycosylase MltE. The active site of bLysG contains a unique structural and sequence signature (DxxQSSES+S) that is important for coordinating a catalytic water. Molecular modeling suggests that the bLysG domain may recognize glycan in a similar manner to MltE. The C-terminal NlpC/P60 domain contains a conserved active site (Cys-His-His-Tyr) that appears to be specific to murein tetrapeptide. Access to the active site is likely regulated by isomerism of a side chain atop the catalytic cysteine, allowing substrate entry or product release (open state), or catalysis (closed state).
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