TY  - JOUR
A1  - Doeven, Mark K.
A1  - Abele, Rupert
A1  - Tampé, Robert
A1  - Poolman, Bert
T1  - The binding specificity of OppA determines the selectivity of the oligopeptide ATP-binding cassette transporter
T2  - Journal of biological chemistry
N2  - 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.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/76140
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-761405
SN  - 0021-9258
VL  - 279
IS  - 31
SP  - 32301
EP  - 32307
PB  - American Society for Biochemistry and Molecular Biology Publications
CY  - Bethesda, Md
ER  -