1G6H

CRYSTAL STRUCTURE OF THE ADP CONFORMATION OF MJ1267, AN ATP-BINDING CASSETTE OF AN ABC TRANSPORTER

1G6H の概要

• エントリーDOI: 10.2210/pdb1g6h/pdb
• 分子名称: HIGH-AFFINITY BRANCHED-CHAIN AMINO ACID TRANSPORT ATP-BINDING PROTEIN, MAGNESIUM ION, METHYL MERCURY ION, ... (5 entities in total)
• 機能のキーワード: beta-core domain, abc specific-beta-strand domain alpha-helix domain, transport protein
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29685.85

構造登録者

Yuan, Y.-R.,Martsinkevich, O.,Karpowich, N.,Millen, L.,Thomas, P.J.,Hunt, J.F. (登録日: 2000-11-06, 公開日: 2001-07-18, 最終更新日: 2024-02-07)

主引用文献

Karpowich, N.,Martsinkevich, O.,Millen, L.,Yuan, Y.R.,Dai, P.L.,MacVey, K.,Thomas, P.J.,Hunt, J.F.
Crystal structures of the MJ1267 ATP binding cassette reveal an induced-fit effect at the ATPase active site of an ABC transporter.
Structure, 9:571-586, 2001

PubMed Abstract: ATP binding cassette (ABC) transporters are ubiquitously distributed transmembrane solute pumps that play a causative role in numerous diseases. Previous structures have defined the fold of the ABC and established the flexibility of its alpha-helical subdomain. But the nature of the mechanical changes that occur at each step of the chemical ATPase cycle have not been defined.

PubMed: 11470432
DOI: 10.1016/S0969-2126(01)00617-7

実験手法

X-RAY DIFFRACTION (1.6 Å)