Journal Article

PUBDB-2018-03872

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png Tripeptide binding in a proton-dependent oligopeptide transporter

Martinez Molledo, M.CSSB*EMBL* ; Quistgaard, E. M. ; Loew, C. (Corresponding author)CSSB*EMBL*

2018
Wiley Chichester

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Please use a persistent id in citations: doi:10.1002/1873-3468.13246  doi:10.3204/PUBDB-2018-03872

Abstract: Proton‐dependent oligopeptide transporters (POTs) are important for the uptake of di‐/tripeptides in many organisms and for drug transport in humans. The binding mode of dipeptides has been well described. However, it is still debated how tripeptides are recognized. Here, we show that tripeptides of the sequence Phe‐Ala‐Xxx bind with similar affinities as dipeptides to the POT transporter from Streptococcus thermophilus (PepT$_{St}$). We furthermore determined a 2.3‐Å structure of PepT$_{St}$ in complex with Phe‐Ala‐Gln. The phenylalanine and alanine residues of the peptide adopt the same positions as previously observed for the Phe‐Ala dipeptide, while the glutamine side chain extends into a hitherto uncharacterized pocket. This pocket is adaptable in size and can likely accommodate a wide variety of peptide side chains.

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Contributing Institute(s):

1. CSSB-EMBL (CSSB-EMBL)
2. EMBL (EMBL)
3. CSSB-EMBL-CL (CSSB-EMBL-CL)

Research Program(s):

1. 6G3 - PETRA III (POF3-622) (POF3-622)
2. SWEDEN-DESY - SWEDEN-DESY Collaboration (2020_Join2-SWEDEN-DESY) (2020_Join2-SWEDEN-DESY)

Experiment(s):

1. PETRA Beamline P14 (PETRA III)

Appears in the scientific report 2018

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Database coverage:
; ; ; BIOSIS Previews ; Clarivate Analytics Master Journal List ; Current Contents - Life Sciences ; Ebsco Academic Search ; IF < 5 ; JCR ; NCBI Molecular Biology Database ; SCOPUS ; Science Citation Index ; Science Citation Index Expanded ; Web of Science Core Collection

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