5UHS

Structure of a SemiSWEET D57A mutant

5UHS の概要

• エントリーDOI: 10.2210/pdb5uhs/pdb
• 関連するPDBエントリー: 5UHQ
• 分子名称: Sugar transporter SemiSWEET, MONOVACCENIN, beta-D-glucopyranose (3 entities in total)
• 機能のキーワード: membrane, transporter, semisweet, transport protein
• 由来する生物種: Leptospira biflexa serovar Patoc (strain Patoc 1 / ATCC 23582 / Paris)
• 細胞内の位置: Cell membrane ; Multi-pass membrane protein : B0SR19
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22254.72

構造登録者

Fastman, N.M.,Feng, L. (登録日: 2017-01-11, 公開日: 2017-08-02, 最終更新日: 2023-10-04)

主引用文献

Latorraca, N.R.,Fastman, N.M.,Venkatakrishnan, A.J.,Frommer, W.B.,Dror, R.O.,Feng, L.
Mechanism of Substrate Translocation in an Alternating Access Transporter.
Cell, 169:96-107.e12, 2017

PubMed Abstract: Transporters shuttle molecules across cell membranes by alternating among distinct conformational states. Fundamental questions remain about how transporters transition between states and how such structural rearrangements regulate substrate translocation. Here, we capture the translocation process by crystallography and unguided molecular dynamics simulations, providing an atomic-level description of alternating access transport. Simulations of a SWEET-family transporter initiated from an outward-open, glucose-bound structure reported here spontaneously adopt occluded and inward-open conformations. Strikingly, these conformations match crystal structures, including our inward-open structure. Mutagenesis experiments further validate simulation predictions. Our results reveal that state transitions are driven by favorable interactions formed upon closure of extracellular and intracellular "gates" and by an unfavorable transmembrane helix configuration when both gates are closed. This mechanism leads to tight allosteric coupling between gates, preventing them from opening simultaneously. Interestingly, the substrate appears to take a "free ride" across the membrane without causing major structural rearrangements in the transporter.

PubMed: 28340354
DOI: 10.1016/j.cell.2017.03.010

実験手法

X-RAY DIFFRACTION (2.8 Å)