1BOW

MULTIDRUG-BINDING DOMAIN OF TRANSCRIPTION ACTIVATOR BMRR (APO FORM)

1BOW の概要

• エントリーDOI: 10.2210/pdb1bow/pdb
• 分子名称: MULTIDRUG-EFFLUX TRANSPORTER 1 REGULATOR BMRR, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: transcription activator, multidrug binding
• 由来する生物種: Bacillus subtilis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 18546.99

構造登録者

Zheleznova, E.E.,Markham, P.N.,Neyfakh, A.A.,Brennan, R.G. (登録日: 1998-08-06, 公開日: 1999-08-06, 最終更新日: 2024-02-07)

主引用文献

Zheleznova, E.E.,Markham, P.N.,Neyfakh, A.A.,Brennan, R.G.
Structural basis of multidrug recognition by BmrR, a transcription activator of a multidrug transporter.
Cell(Cambridge,Mass.), 96:353-362, 1999

PubMed Abstract: Multidrug-efflux transporters demonstrate an unusual ability to recognize multiple structurally dissimilar toxins. A comparable ability to bind diverse hydrophobic cationic drugs is characteristic of the Bacillus subtilis transcription regulator BmrR, which upon drug binding activates expression of the multidrug transporter Bmr. Crystal structures of the multidrug-binding domain of BmrR (2.7 A resolution) and of its complex with the drug tetraphenylphosphonium (2.8 A resolution) revealed a drug-induced unfolding and relocation of an alpha helix, which exposes an internal drug-binding pocket. Tetraphenylphosphonium binding is mediated by stacking and van der Waals contacts with multiple hydrophobic residues of the pocket and by an electrostatic interaction between the positively charged drug and a buried glutamate residue, which is the key to cation selectivity. Similar binding principles may be used by other multidrug-binding proteins.

PubMed: 10025401
DOI: 10.1016/S0092-8674(00)80548-6

実験手法

X-RAY DIFFRACTION (2.7 Å)