6F2W

Bacterial asc transporter crystal structure in open to in conformation

6F2W の概要

• エントリーDOI: 10.2210/pdb6f2w/pdb
• 関連するPDBエントリー: 6F2G
• 分子名称: Putative amino acid/polyamine transport protein, Nanobody 74, ALPHA-AMINOISOBUTYRIC ACID, ... (4 entities in total)
• 機能のキーワード: leut fold, lat transporter, apc transporter, transport protein
• 由来する生物種: Carnobacterium sp. AT7; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 62188.92

構造登録者

Fort, J.,Errasti-Murugarren, E.,Carpena, X.,Palacin, M.,Fita, I. (登録日: 2017-11-27, 公開日: 2019-04-24, 最終更新日: 2024-01-17)

主引用文献

Errasti-Murugarren, E.,Fort, J.,Bartoccioni, P.,Diaz, L.,Pardon, E.,Carpena, X.,Espino-Guarch, M.,Zorzano, A.,Ziegler, C.,Steyaert, J.,Fernandez-Recio, J.,Fita, I.,Palacin, M.
L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction.
Nat Commun, 10:1807-1807, 2019

PubMed Abstract: L-amino acid transporters (LATs) play key roles in human physiology and are implicated in several human pathologies. LATs are asymmetric amino acid exchangers where the low apparent affinity cytoplasmic side controls the exchange of substrates with high apparent affinity on the extracellular side. Here, we report the crystal structures of an LAT, the bacterial alanine-serine-cysteine exchanger (BasC), in a non-occluded inward-facing conformation in both apo and substrate-bound states. We crystallized BasC in complex with a nanobody, which blocks the transporter from the intracellular side, thus unveiling the sidedness of the substrate interaction of BasC. Two conserved residues in human LATs, Tyr 236 and Lys 154, are located in equivalent positions to the Na1 and Na2 sites of sodium-dependent APC superfamily transporters. Functional studies and molecular dynamics (MD) calculations reveal that these residues are key for the asymmetric substrate interaction of BasC and in the homologous human transporter Asc-1.

PubMed: 31000719
DOI: 10.1038/s41467-019-09837-z

実験手法

X-RAY DIFFRACTION (3.4 Å)