6ghj

PepTSt in complex with tripeptide Phe-Ala-Gln

spinqualitylabelsall models 6ghj, resolution 2.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ghj is a 2 chain structure with sequence from Strt2 and Synthetic construct sequences. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1PE, 78M, 78N, EPE, NA, PO4 Gene: dtpT, stu0970 (STRT2) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Proton-dependent oligopeptide transporters (POTs) are important for 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 (PepTSt ). We furthermore determined a 2.3-A structure of PepTSt 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. This article is protected by copyright. All rights reserved. Tripeptide binding in a Proton-Dependent Oligopeptide Transporter.,Martinez Molledo M, Quistgaard EM, Low C FEBS Lett. 2018 Sep 8. doi: 10.1002/1873-3468.13246. PMID:30194725 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Symporter

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