3PUW

Crystal Structure of an outward-facing MBP-Maltose transporter complex bound to ADP-AlF4

3PUW の概要

• エントリーDOI: 10.2210/pdb3puw/pdb
• 関連するPDBエントリー: 3RLF 3puv 3pux 3puy 3puz 3pv0
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose-binding periplasmic protein, TETRAFLUOROALUMINATE ION, Maltose transport system permease protein malF, ... (11 entities in total)
• 機能のキーワード: atp binding cassette nucleotide binding domain substrate binding protein transmembrane domain, abc transporter importer atpase, atp binding maltodextrin binding, transmembrane integral membrane, 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: 224728.16

構造登録者

Oldham, M.L.,Chen, J. (登録日: 2010-12-06, 公開日: 2011-08-10, 最終更新日: 2024-02-21)

主引用文献

Oldham, M.L.,Chen, J.
Snapshots of the maltose transporter during ATP hydrolysis.
Proc.Natl.Acad.Sci.USA, 108:15152-15156, 2011

PubMed Abstract: ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(β,γ-imido)triphosphate or ADP in conjunction with phosphate analogs BeF(3)(-), VO(4)(3-), or AIF(4)(-), were determined to 2.2- to 2.4-Å resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.

PubMed: 21825153
DOI: 10.1073/pnas.1108858108

実験手法

X-RAY DIFFRACTION (2.3 Å)