5OXK

PepTSt in complex with dipeptide Ala-Gln

5OXK の概要

• エントリーDOI: 10.2210/pdb5oxk/pdb
• 分子名称: Di-or tripeptide:H+ symporter, PHOSPHATE ION, PENTAETHYLENE GLYCOL, ... (8 entities in total)
• 機能のキーワード: alpha helical membrane protein, mfs fold, membrane protein, peptide transporter, transport protein
• 由来する生物種: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 58494.48

構造登録者

Martinez Molledo, M.,Quistgaard, E.M.,Loew, C. (登録日: 2017-09-07, 公開日: 2018-02-21, 最終更新日: 2024-01-17)

主引用文献

Martinez Molledo, M.,Quistgaard, E.M.,Flayhan, A.,Pieprzyk, J.,Low, C.
Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter.
Structure, 26:467-476.e4, 2018

PubMed Abstract: Proton-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 PepT from Streptococcus thermophilus, and structures were determined of PepT 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 PepT 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.

PubMed: 29429879
DOI: 10.1016/j.str.2018.01.005

実験手法

X-RAY DIFFRACTION (2.38 Å)