4LEP

Structural insights into substrate recognition in proton dependent oligopeptide transporters

4LEP の概要

• エントリーDOI: 10.2210/pdb4lep/pdb
• 分子名称: Proton:oligopeptide symporter POT family, N-[(1R)-1-phosphonoethyl]-L-alaninamide, ZINC ION (3 entities in total)
• 機能のキーワード: mfs superfamily, peptide transporter, membrane protein, tranport protein
• 由来する生物種: Shewanella oneidensis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 114906.00

構造登録者

Guettou, F.,Quistgaard, E.M.,Tresaugues, L.,Moberg, P.,Jegerschold, C.,Zhu, L.,Jong, A.J.,Nordlund, P.,Low, C. (登録日: 2013-06-26, 公開日: 2013-07-10, 最終更新日: 2024-02-28)

主引用文献

Guettou, F.,Quistgaard, E.M.,Tresaugues, L.,Moberg, P.,Jegerschold, C.,Zhu, L.,Jong, A.J.,Nordlund, P.,Low, C.
Structural insights into substrate recognition in proton-dependent oligopeptide transporters.
Embo Rep., 14:804-810, 2013

PubMed Abstract: Short-chain peptides are transported across membranes through promiscuous proton-dependent oligopeptide transporters (POTs)--a subfamily of the major facilitator superfamily (MFS). The human POTs, PEPT1 and PEPT2, are also involved in the absorption of various drugs in the gut as well as transport to target cells. Here, we present a structure of an oligomeric POT transporter from Shewanella oneidensis (PepTSo2), which was crystallized in the inward open conformation in complex with the peptidomimetic alafosfalin. All ligand-binding residues are highly conserved and the structural insights presented here are therefore likely to also apply to human POTs.

PubMed: 23867627
DOI: 10.1038/embor.2013.107

実験手法

X-RAY DIFFRACTION (3.2 Å)