1PV7

Crystal structure of lactose permease with TDG

1PV7 の概要

• エントリーDOI: 10.2210/pdb1pv7/pdb
• 関連するPDBエントリー: 1PV6
• 関連するBIRD辞書のPRD_ID: PRD_900027
• 分子名称: Lactose permease, beta-D-galactopyranose-(1-1)-1-thio-beta-D-galactopyranose (2 entities in total)
• 機能のキーワード: transport, sugar transport, symport, membrane protein, transport protein
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93686.32

構造登録者

Abramson, J.,Smirnova, I.,Kasho, V.,Verner, G.,Kaback, H.R.,Iwata, S. (登録日: 2003-06-26, 公開日: 2003-08-12, 最終更新日: 2024-05-29)

主引用文献

Abramson, J.,Smirnova, I.,Kasho, V.,Verner, G.,Kaback, H.R.,Iwata, S.
Structure and mechanism of the lactose permease of Escherichia coli
SCIENCE, 301:610-615, 2003

PubMed Abstract: Membrane transport proteins that transduce free energy stored in electrochemical ion gradients into a concentration gradient are a major class of membrane proteins. We report the crystal structure at 3.5 angstroms of the Escherichia coli lactose permease, an intensively studied member of the major facilitator superfamily of transporters. The molecule is composed of N- and C-terminal domains, each with six transmembrane helices, symmetrically positioned within the permease. A large internal hydrophilic cavity open to the cytoplasmic side represents the inward-facing conformation of the transporter. The structure with a bound lactose homolog, beta-D-galactopyranosyl-1-thio-beta-D-galactopyranoside, reveals the sugar-binding site in the cavity, and residues that play major roles in substrate recognition and proton translocation are identified. We propose a possible mechanism for lactose/proton symport (co-transport) consistent with both the structure and a large body of experimental data.

PubMed: 12893935
DOI: 10.1126/science.1088196

実験手法

X-RAY DIFFRACTION (3.6 Å)