ArticleThe Journal of biological chemistry2011
Compensating stereochemical changes allow murein tripeptide to be accommodated in a conventional peptide-binding protein.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 45 citations in OpenAlex.
- A conserved hub protein required for peptidoglycan remodeling and cell division inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Defined roles for the Staphylococcus aureus POT transporter DtpT in di/tripeptide uptake and glutathione utilisation inside human macrophages.PLoS pathogens · 2025Article
- Itaconate utilisation by the human pathogen Pseudomonas aeruginosa requires uptake via the IctPQM TRAP transporter.The Biochemical journal · 2025Article
- Structural characterization of the ABC transporter DppABCDF in Escherichia coli reveals insights into dipeptide acquisition.PLoS biology · 2025Article
- Structure and ligand binding in the putative anti-microbial peptide transporter protein, YejA.Microbiology (Reading, England) · 2024Article
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- Characterization of the l-arabinofuranose-specific GafABCD ABC transporter essential for l-arabinose-dependent growth of the lignocellulose-degrading bacteriumMicrobiology (Reading, England) · 2023Article
- Microbial Musings - Winter 2022.Microbiology (Reading, England) · 2022Article
- TheMicrobiology (Reading, England) · 2020Article
- Microbial Musings - October 2020.Microbiology (Reading, England) · 2020Article
- Peptidoglycan Sensing Prevents Quiescence and Promotes Quorum-Independent Colony Growth of Uropathogenic Escherichia coli.Journal of bacteriology · 2020Article
- Chlamydia trachomatis Oligopeptide Transporter Performs Dual Functions of Oligopeptide Transport and Peptidoglycan Recycling.Infection and immunity · 2020Article
- Competent but complex communication: The phenomena of pheromone-responsive plasmids.PLoS pathogens · 2020Review
- Molecular Basis of Unexpected Specificity of ABC Transporter-Associated Substrate-Binding Protein DppA from Helicobacter pylori.Journal of bacteriology · 2019Article
- Crystal structure of the putative peptide-binding protein AppA from Clostridium difficile.Acta crystallographica. Section F, Structural biology communications · 2019Article
- Open Conformation of theBiology · 2018Article
- Genome scale identification, structural analysis, and classification of periplasmic binding proteins from Mycobacterium tuberculosis.Current genetics · 2017Article
- c-di-AMP modulates Listeria monocytogenes central metabolism to regulate growth, antibiotic resistance and osmoregulation.Molecular microbiology · 2017Article
- The effects of methionine acquisition and synthesis on Streptococcus pneumoniae growth and virulence.PloS one · 2013Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
The oligopeptide permease (Opp) of Escherichia coli is an ATP-binding cassette transporter that uses the substrate-binding protein (SBP) OppA to bind peptides and deliver them to the membrane components (OppBCDF) for transport. OppA binds conventional peptides 2-5 residues in length regardless of their sequence, but does not facilitate transport of the cell wall component murein tripeptide (Mtp, L-Ala-γ-D-Glu-meso-Dap), which contains a D-amino acid and a γ-peptide linkage. Instead, MppA, a homologous substrate-binding protein, forms a functional transporter with OppBCDF for uptake of this unusual tripeptide. Here we have purified MppA and demonstrated biochemically that it binds Mtp with high affinity (K(D) ∼ 250 nM). The crystal structure of MppA in complex with Mtp has revealed that Mtp is bound in a relatively extended conformation with its three carboxylates projecting from one side of the molecule and its two amino groups projecting from the opposite face. Specificity for Mtp is conferred by charge-charge and dipole-charge interactions with ionic and polar residues of MppA. Comparison of the structure of MppA-Mtp with structures of conventional tripeptides bound to OppA, reveals that the peptide ligands superimpose remarkably closely given the profound differences in their structures. Strikingly, the effect of the D-stereochemistry, which projects the side chain of the D-Glu residue at position 2 in the direction of the main chain in a conventional tripeptide, is compensated by the formation of a γ-linkage to the amino group of diaminopimelic acid, mimicking the peptide bond between residues 2 and 3 of a conventional tripeptide.
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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.