4LLH

Substrate bound outward-open state of the symporter BetP

4LLH の概要

• エントリーDOI: 10.2210/pdb4llh/pdb
• 分子名称: Glycine betaine transporter BetP, 2-(trimethyl-lambda~5~-arsanyl)ethanol, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: secondary transporter, transport protein
• 由来する生物種: Corynebacterium glutamicum
• 細胞内の位置: Cell membrane; Multi-pass membrane protein: P54582
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 185269.66

構造登録者

Perez, C.,Faust, B.,Ziegler, C. (登録日: 2013-07-09, 公開日: 2014-05-07, 最終更新日: 2024-02-28)

主引用文献

Perez, C.,Faust, B.,Mehdipour, A.R.,Francesconi, K.A.,Forrest, L.R.,Ziegler, C.
Substrate-bound outward-open state of the betaine transporter BetP provides insights into Na(+) coupling.
Nat Commun, 5:4231-4231, 2014

PubMed Abstract: The Na(+)-coupled betaine symporter BetP shares a highly conserved fold with other sequence unrelated secondary transporters, for example, with neurotransmitter symporters. Recently, we obtained atomic structures of BetP in distinct conformational states, which elucidated parts of its alternating-access mechanism. Here, we report a structure of BetP in a new outward-open state in complex with an anomalous scattering substrate, adding a fundamental piece to an unprecedented set of structural snapshots for a secondary transporter. In combination with molecular dynamics simulations these structural data highlight important features of the sequential formation of the substrate and sodium-binding sites, in which coordinating water molecules play a crucial role. We observe a strictly interdependent binding of betaine and sodium ions during the coupling process. All three sites undergo progressive reshaping and dehydration during the alternating-access cycle, with the most optimal coordination of all substrates found in the closed state.

PubMed: 25023443
DOI: 10.1038/ncomms5231

実験手法

X-RAY DIFFRACTION (2.8 Å)