6LH0

Crystal structure of a cysteine-pair mutant (P10C-S291C) of a bacterial bile acid transporter in an inward-facing apo-state

6LH0 の概要

• エントリーDOI: 10.2210/pdb6lh0/pdb
• 関連するPDBエントリー: 6LGV 6LGY 6LGZ
• 分子名称: Transporter, sodium/bile acid symporter family, 2,3-dihydroxypropyl (9Z)-octadec-9-enoate (3 entities in total)
• 機能のキーワード: bile acid transporter, asbt, ntcp, slc10, transport protein
• 由来する生物種: Yersinia frederiksenii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 34457.52

構造登録者

Wang, X.,Lyu, Y.,Ji, Y.,Sun, Z.,Zhou, X. (登録日: 2019-12-06, 公開日: 2020-12-09, 最終更新日: 2024-11-20)

主引用文献

Wang, X.,Lyu, Y.,Ji, Y.,Sun, Z.,Zhou, X.
Substrate binding in the bile acid transporter ASBT Yf from Yersinia frederiksenii.
Acta Crystallogr D Struct Biol, 77:117-125, 2021

PubMed Abstract: Apical sodium-dependent bile acid transporter (ASBT) retrieves bile acids from the small intestine and plays a pivotal role in enterohepatic circulation. Currently, high-resolution structures are available for two bacterial ASBT homologs (ASBT from Neisseria meningitides and ASBT from Yersinia frederiksenii), from which an elevator-style alternating-access mechanism has been proposed for substrate transport. A key concept in this model is that the substrate binds to the central cavity of the transporter so that the elevator-like motion can expose the bound substrate alternatingly to either side of the membrane during a transport cycle. However, no structure of an ASBT has been solved with a substrate bound in its central cavity, so how a substrate binds to ASBT remains to be defined. In this study, molecular docking, structure determination and functional analysis were combined to define and validate the details of substrate binding in ASBT. The findings provide coherent evidence to provide a clearer picture of how the substrate binds in the central cavity of ASBT that fits the alternating-access model.

PubMed: 33404531
DOI: 10.1107/S2059798320015004

実験手法

X-RAY DIFFRACTION (2.812 Å)