4D2C

Structure of a di peptide bound POT family peptide transporter

4D2C の概要

• エントリーDOI: 10.2210/pdb4d2c/pdb
• 関連するPDBエントリー: 4D2B 4D2D
• 分子名称: Di-or tripeptide:H+ symporter, (2S)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, (2R)-2,3-DIHYDROXYPROPYL(7Z)-PENTADEC-7-ENOATE, ... (7 entities in total)
• 機能のキーワード: transport protein, major facilitator superfamily, proton oligopeptide transporter (pot) family, peptide transporter, peptide complex
• 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: 55957.14

構造登録者

Lyons, J.A.,Parker, J.L.,Solcan, N.,Brinth, A.,Li, D.,Shah, S.T.A.,Caffrey, M.,Newstead, S. (登録日: 2014-05-09, 公開日: 2014-06-25, 最終更新日: 2023-12-20)

主引用文献

Lyons, J.A.,Parker, J.L.,Solcan, N.,Brinth, A.,Li, D.,Shah, S.T.,Caffrey, M.,Newstead, S.
Structural Basis for Polyspecificity in the Pot Family of Proton-Coupled Oligopeptide Transporters.
Embo Rep., 15:886-, 2014

PubMed Abstract: An enigma in the field of peptide transport is the structural basis for ligand promiscuity, as exemplified by PepT1, the mammalian plasma membrane peptide transporter. Here, we present crystal structures of di- and tripeptide-bound complexes of a bacterial homologue of PepT1, which reveal at least two mechanisms for peptide recognition that operate within a single, centrally located binding site. The dipeptide was orientated laterally in the binding site, whereas the tripeptide revealed an alternative vertical binding mode. The co-crystal structures combined with functional studies reveal that biochemically distinct peptide-binding sites likely operate within the POT/PTR family of proton-coupled symporters and suggest that transport promiscuity has arisen in part through the ability of the binding site to accommodate peptides in multiple orientations for transport.

PubMed: 24916388
DOI: 10.15252/EMBR.201338403

実験手法

X-RAY DIFFRACTION (2.47 Å)