The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter

  • The purification and functional reconstitution of a five-component oligopeptide ATP-binding cassette transporter with a remarkably wide substrate specificity are described. High-affinity peptide uptake was dependent on liganded substrate-binding protein OppA, which interacts with the translocator OppBCDF with higher affinity than unliganded OppA. Transport screening with combinatorial peptide libraries revealed that (i) the Opp transporter is not selective with respect to amino acid side chains of the transported peptides; (ii) any peptide that can bind to OppA is transported via Opp, including very long peptides up to 35 residues long; and (iii) the binding specificity of OppA largely determines the overall transport selectivity.

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Author:Mark K. Doeven, Rupert AbeleORCiDGND, Robert TampéORCiDGND, Bert PoolmanORCiDGND
URN:urn:nbn:de:hebis:30:3-761405
DOI:https://doi.org/10.1074/jbc.M404343200
ISSN:0021-9258
Pubmed Id:https://pubmed.ncbi.nlm.nih.gov/15169767
Parent Title (English):Journal of biological chemistry
Publisher:American Society for Biochemistry and Molecular Biology Publications
Place of publication:Bethesda, Md
Document Type:Article
Language:English
Date of Publication (online):2021/01/04
Year of first Publication:2004
Publishing Institution:Universitätsbibliothek Johann Christian Senckenberg
Release Date:2023/11/09
Volume:279
Issue:31
Page Number:7
First Page:32301
Last Page:32307
HeBIS-PPN:51650701X
Institutes:Biochemie, Chemie und Pharmazie
Dewey Decimal Classification:5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie
Sammlungen:Universitätspublikationen
Licence (German):License LogoCreative Commons - CC BY - Namensnennung 4.0 International

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