ArticleJournal of bacteriology2013
Structure and function of a novel LD-carboxypeptidase a involved in peptidoglycan recycling.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 21 citations in OpenAlex.
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- Hijacking the Peptidoglycan Recycling Pathway of Escherichia coli to Produce Muropeptides.Chemistry (Weinheim an der Bergstrasse, Germany) · 2023Article
- Pseudomonas aeruginosa Alters Peptidoglycan Composition under Nutrient Conditions Resembling Cystic Fibrosis Lung Infections.mSystems · 2022Article
- Elucidation of host and symbiont contributions to peptidoglycan metabolism based on comparative genomics of eight aphid subfamilies and their Buchnera.PLoS genetics · 2022Article
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- Selective Inhibition ofAntimicrobial agents and chemotherapy · 2018Article
- Cell-Wall Recycling of the Gram-Negative Bacteria and the Nexus to Antibiotic Resistance.Chemical reviews · 2018Review
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- Fungal lifestyle reflected in serine protease repertoire.Scientific reports · 2017Article
- The Cell Shape-determining Csd6 Protein from Helicobacter pylori Constitutes a New Family of L,D-Carboxypeptidase.The Journal of biological chemistry · 2015Article
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- Structure-guided functional characterization of DUF1460 reveals a highly specific NlpC/P60 amidase family.Structure (London, England : 1993) · 2014Article
Corrections and comments
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Authors and funding
14 authors at 6 institutions in 2 countries.
Funding
Abstract
Approximately 50% of cell wall peptidoglycan in Gram-negative bacteria is recycled with each generation. The primary substrates used for peptidoglycan biosynthesis and recycling in the cytoplasm are GlcNAc-MurNAc(anhydro)-tetrapeptide and its degradation product, the free tetrapeptide. This complex process involves ∼15 proteins, among which the cytoplasmic enzyme ld-carboxypeptidase A (LdcA) catabolizes the bond between the last two l- and d-amino acid residues in the tetrapeptide to form the tripeptide, which is then utilized as a substrate by murein peptide ligase (Mpl). LdcA has been proposed as an antibacterial target. The crystal structure of Novosphingobium aromaticivorans DSM 12444 LdcA (NaLdcA) was determined at 1.89-Å resolution. The enzyme was biochemically characterized and its interactions with the substrate modeled, identifying residues potentially involved in substrate binding. Unaccounted electron density at the dimer interface in the crystal suggested a potential site for disrupting protein-protein interactions should a dimer be required to perform its function in bacteria. Our analysis extends the identification of functional residues to several other homologs, which include enzymes from bacteria that are involved in hydrocarbon degradation and destruction of coral reefs. The NaLdcA crystal structure provides an alternate system for investigating the structure-function relationships of LdcA and increases the structural coverage of the protagonists in bacterial cell wall recycling.
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Registered trials
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