3BRY

Crystal structure of the Ralstonia pickettii toluene transporter TbuX

3BRY の概要

• エントリーDOI: 10.2210/pdb3bry/pdb
• 関連するPDBエントリー: 3BRZ 3BS0
• 分子名称: TbuX, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (2 entities in total)
• 機能のキーワード: beta barrel, outer membrane protein, transport protein
• 由来する生物種: Ralstonia pickettii
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 93166.16

構造登録者

Hearn, E.M.,Patel, D.R.,van den Berg, B. (登録日: 2007-12-21, 公開日: 2008-06-10, 最終更新日: 2024-02-21)

主引用文献

Hearn, E.M.,Patel, D.R.,van den Berg, B.
Outer-membrane transport of aromatic hydrocarbons as a first step in biodegradation.
Proc.Natl.Acad.Sci.Usa, 105:8601-8606, 2008

PubMed Abstract: Bacterial biodegradation of hydrocarbons, an important process for environmental remediation, requires the passage of hydrophobic substrates across the cell membrane. Here, we report crystal structures of two outer membrane proteins, Pseudomonas putida TodX and Ralstonia pickettii TbuX, which have been implicated in hydrocarbon transport and are part of a subfamily of the FadL fatty acid transporter family. The structures of TodX and TbuX show significant differences with those previously determined for Escherichia coli FadL, which may provide an explanation for the substrate-specific transport of TodX and TbuX observed with in vivo transport assays. The TodX and TbuX structures revealed 14-stranded beta-barrels with an N-terminal hatch domain blocking the barrel interior. A hydrophobic channel with bound detergent molecules extends from the extracellular surface and is contiguous with a passageway through the hatch domain, lined by both hydrophobic and polar or charged residues. The TodX and TbuX structures support a mechanism for transport of hydrophobic substrates from the extracellular environment to the periplasm via a channel through the hatch domain.

PubMed: 18559855
DOI: 10.1073/pnas.0801264105

実験手法

X-RAY DIFFRACTION (3.2 Å)