2R6G

The Crystal Structure of the E. coli Maltose Transporter

2R6G の概要

• エントリーDOI: 10.2210/pdb2r6g/pdb
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose/maltodextrin import ATP-binding protein malK, Maltose-binding periplasmic protein, Maltose transport system permease protein malF, ... (6 entities in total)
• 機能のキーワード: abc transporter, catalytic intermediate, e. coli maltose transporter, mbp, maltodextrin binding protein, malk, atp binding cassette, atp-binding, hydrolase, inner membrane, membrane, nucleotide-binding, sugar transport, transmembrane, hydrolase-transport protein complex, hydrolase/transport protein
• 由来する生物種: Escherichia coli; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 215776.04

構造登録者

Oldham, M.L.,Khare, D.,Quiocho, F.A.,Davidson, A.L.,Chen, J. (登録日: 2007-09-05, 公開日: 2007-11-27, 最終更新日: 2023-08-30)

主引用文献

Oldham, M.L.,Khare, D.,Quiocho, F.A.,Davidson, A.L.,Chen, J.
Crystal structure of a catalytic intermediate of the maltose transporter.
Nature, 450:515-521, 2007

PubMed Abstract: The maltose uptake system of Escherichia coli is a well-characterized member of the ATP-binding cassette transporter superfamily. Here we present the 2.8-A crystal structure of the intact maltose transporter in complex with the maltose-binding protein, maltose and ATP. This structure, stabilized by a mutation that prevents ATP hydrolysis, captures the ATP-binding cassette dimer in a closed, ATP-bound conformation. Maltose is occluded within a solvent-filled cavity at the interface of the two transmembrane subunits, about halfway into the lipid bilayer. The binding protein docks onto the entrance of the cavity in an open conformation and serves as a cap to ensure unidirectional translocation of the sugar molecule. These results provide direct evidence for a concerted mechanism of transport in which solute is transferred from the binding protein to the transmembrane subunits when the cassette dimer closes to hydrolyse ATP.

PubMed: 18033289
DOI: 10.1038/nature06264

実験手法

X-RAY DIFFRACTION (2.8 Å)