ArticleThe Journal of biological chemistry2015
Loss of a Functionally and Structurally Distinct ld-Transpeptidase, LdtMt5, Compromises Cell Wall Integrity in Mycobacterium tuberculosis.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
29 citing papers in PubMed, 55 citations in OpenAlex.
- Peptide Mimetic Platform for Activity Profiling of Mycobacterial l,d-Transpeptidases.Biochemistry · 2026Article
- Activity Profiling of Mycobacterial L,D-Transpeptidases.bioRxiv : the preprint server for biology · 2026Article
- Peptidoglycan LD-Transpeptidases.Antibiotics (Basel, Switzerland) · 2025Review
- Origin, Evolution and Diversity of φ29-like Phages-Review and Bioinformatic Analysis.International journal of molecular sciences · 2024Review
- Article
- Article
- LdtC Is a Key l,d-Transpeptidase for Peptidoglycan Assembly in Mycobacterium smegmatis.Journal of bacteriology · 2023Article
- A pro-oxidant property of vitamin C to overcome the burden of latentFrontiers in cellular and infection microbiology · 2023Review
- The l,d-Transpeptidase LdtACS infectious diseases · 2022Article
- Structure-Activity Relationship of Penem Antibiotic Side Chains Used against Mycobacteria Reveals Highly Active Compounds.ACS infectious diseases · 2022Article
- Peptidoglycan compositional analysis of Mycobacterium smegmatis using high-resolution LC-MS.Scientific reports · 2022Article
- T405, a New Penem, ExhibitsAntimicrobial agents and chemotherapy · 2022Article
- Article
- Competing off-loading mechanisms of meropenem from an l,d-transpeptidase reduce antibiotic effectiveness.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Investigating β-Lactam Drug Targets inACS infectious diseases · 2021Article
- Complete Genome Sequence of the Newly DevelopedFrontiers in microbiology · 2021Article
- Analysis of β-lactone formation by clinically observed carbapenemases informs on a novel antibiotic resistance mechanism.The Journal of biological chemistry · 2020Article
- Building peptidoglycan inside eukaryotic cells: A view from symbiotic and pathogenic bacteria.Molecular microbiology · 2020Review
- Phylogenetic and Biochemical Analyses of Mycobacterial l,d-Transpeptidases Reveal a Distinct Enzyme Class That Is Preferentially Acylated by Meropenem.ACS infectious diseases · 2019Article
- Identification of potent L,D-transpeptidase 5 inhibitors for Mycobacterium tuberculosis as potential anti-TB leads: virtual screening and molecular dynamics simulations.Journal of molecular modeling · 2019Article
Corrections and comments
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
The final step of peptidoglycan (PG) biosynthesis in bacteria involves cross-linking of peptide side chains. This step in Mycobacterium tuberculosis is catalyzed by ld- and dd-transpeptidases that generate 3→3 and 4→3 transpeptide linkages, respectively. M. tuberculosis PG is predominantly 3→3 cross-linked, and LdtMt2 is the dominant ld-transpeptidase. There are four additional sequence paralogs of LdtMt2 encoded by the genome of this pathogen, and the reason for this apparent redundancy is unknown. Here, we studied one of the paralogs, LdtMt5, and found it to be structurally and functionally distinct. The structures of apo-LdtMt5 and its meropenem adduct presented here demonstrate that, despite overall architectural similarity to LdtMt2, the LdtMt5 active site has marked differences. The presence of a structurally divergent catalytic site and a proline-rich C-terminal subdomain suggest that this protein may have a distinct role in PG metabolism, perhaps involving other cell wall-anchored proteins. Furthermore, M. tuberculosis lacking a functional copy of LdtMt5 displayed aberrant growth and was more susceptible to killing by crystal violet, osmotic shock, and select carbapenem antibiotics. Therefore, we conclude that LdtMt5 is not a functionally redundant ld-transpeptidase, but rather it serves a unique and important role in maintaining the integrity of the M. tuberculosis cell wall.
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Registered trials
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.