6GHJ

PepTSt in complex with tripeptide Phe-Ala-Gln

6GHJ の概要

• エントリーDOI: 10.2210/pdb6ghj/pdb
• 分子名称: Di-or tripeptide:H+ symporter, PHE-ALA-GLN, PHOSPHATE ION, ... (9 entities in total)
• 機能のキーワード: membrane protein, mfs, pot, peptide transporter
• 由来する生物種: Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 58333.47

構造登録者

Martinez Molledo, M.,Quistgaard, E.M.,Loew, C. (登録日: 2018-05-08, 公開日: 2018-09-19, 最終更新日: 2024-01-17)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.26 Å)