3PV0

Crystal Structure of a pre-translocation state MBP-Maltose transporter complex without nucleotide

3PV0 の概要

• エントリーDOI: 10.2210/pdb3pv0/pdb
• 関連するPDBエントリー: 3puv 3puw 3pux 3puy 3puz
• 関連するBIRD辞書のPRD_ID: PRD_900001
• 分子名称: Maltose transporter subunit; periplasmic-binding component of ABC superfamily, Maltose transporter subunit; membrane component of ABC superfamily, Fused maltose transport subunit, ATP-binding component of ABC superfamily; regulatory protein, ... (6 entities in total)
• 機能のキーワード: atp binding cassette, nucleotide binding domain, substrate binding protein, abc transporter, importer, atpase, atp binding, maltodextrin binding, transmembrane integral membrane, transport protein, membrane 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: 215917.10

構造登録者

Oldham, M.L.,Chen, J. (登録日: 2010-12-06, 公開日: 2011-05-18, 最終更新日: 2024-10-30)

主引用文献

Oldham, M.L.,Chen, J.
Crystal structure of the maltose transporter in a pretranslocation intermediate state.
Science, 332:1202-1205, 2011

PubMed Abstract: Adenosine triphosphate (ATP)-binding cassette (ABC) transporters convert chemical energy from ATP hydrolysis to mechanical work for substrate translocation. They function by alternating between two states, exposing the substrate-binding site to either side of the membrane. A key question that remains to be addressed is how substrates initiate the transport cycle. Using x-ray crystallography, we have captured the maltose transporter in an intermediate step between the inward- and outward-facing states. We show that interactions with substrate-loaded maltose-binding protein in the periplasm induce a partial closure of the MalK dimer in the cytoplasm. ATP binding to this conformation then promotes progression to the outward-facing state. These results, interpreted in light of biochemical and functional studies, provide a structural basis to understand allosteric communication in ABC transporters.

PubMed: 21566157
DOI: 10.1126/science.1200767

実験手法

X-RAY DIFFRACTION (3.1 Å)