6GHJ

PepTSt in complex with tripeptide Phe-Ala-Gln

Summary for 6GHJ

• Entry DOI: 10.2210/pdb6ghj/pdb
• Descriptor: Di-or tripeptide:H+ symporter, PHE-ALA-GLN, PHOSPHATE ION, ... (9 entities in total)
• Functional Keywords: membrane protein, mfs, pot, peptide transporter
• Biological source: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311); More
• Total number of polymer chains: 2
• Total formula weight: 58333.47

Authors

Martinez Molledo, M.,Quistgaard, E.M.,Loew, C. (deposition date: 2018-05-08, release date: 2018-09-19, Last modification date: 2024-01-17)

Primary citation

Martinez Molledo, M.,Quistgaard, E.M.,Low, C.
Tripeptide binding in a proton-dependent oligopeptide transporter.
FEBS Lett., 592:3239-3247, 2018

PubMed 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 ). We furthermore determined a 2.3-Å structure of PepT 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.

PubMed: 30194725
DOI: 10.1002/1873-3468.13246

Experimental method

X-RAY DIFFRACTION (2.26 Å)