5oxp
PepTSt in occluded conformation with phosphate ion boundPepTSt in occluded conformation with phosphate ion bound
Structural highlights
FunctionPublication Abstract from PubMedProton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure. Twenty-eight peptides were screened for binding to PepTSt from Streptococcus thermophilus, and structures were determined of PepTSt in complex with four physicochemically diverse dipeptides, which bind with millimolar affinity: Ala-Leu, Phe-Ala, Ala-Gln, and Asp-Glu. The structures show that PepTSt can adapt to different peptide side chains through movement of binding site residues and water molecules, and that a good fit can be further aided by adjustment of the position of the peptide itself. Finally, structures were also determined in complex with adventitiously bound HEPES, polyethylene glycol, and phosphate molecules, which further underline the adaptability of the binding site. Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter.,Martinez Molledo M, Quistgaard EM, Flayhan A, Pieprzyk J, Low C Structure. 2018 Mar 6;26(3):467-476.e4. doi: 10.1016/j.str.2018.01.005. Epub 2018, Feb 8. PMID:29429879[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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