2QTK

Crystal Structure of the outer membrane protein opdK from Pseudomonas aeruginosa

2QTK の概要

• エントリーDOI: 10.2210/pdb2qtk/pdb
• 分子名称: Probable porin, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE (2 entities in total)
• 機能のキーワード: outer membrane protein, beta barrel, vanillate transport, porin, membrane protein
• 由来する生物種: Pseudomonas aeruginosa
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 92728.68

構造登録者

Biswas, S.,Van den Berg, B. (登録日: 2007-08-02, 公開日: 2008-06-24, 最終更新日: 2024-02-21)

主引用文献

Biswas, S.,Mohammad, M.M.,Movileanu, L.,van den Berg, B.
Crystal Structure of the Outer Membrane Protein OpdK from Pseudomonas aeruginosa.
Structure, 16:1027-1035, 2008

PubMed Abstract: In Gram-negative bacteria that do not have porins, most water-soluble and small molecules are taken up by substrate-specific channels belonging to the OprD family. We report here the X-ray crystal structure of OpdK, an OprD family member implicated in the uptake of vanillate and related small aromatic acids. The OpdK structure reveals a monomeric, 18-stranded beta barrel with a kidney-shaped central pore. The OpdK pore constriction is relatively wide for a substrate-specific channel (approximately 8 A diameter), and it is lined by a positively charged patch of arginine residues on one side and an electronegative pocket on the opposite side-features likely to be important for substrate selection. Single-channel electrical recordings of OpdK show binding of vanillate to the channel, and they suggest that OpdK forms labile trimers in the outer membrane. Comparison of the OpdK structure with that of Pseudomonas aeruginosa OprD provides the first qualitative insights into the different substrate specificities of these closely related channels.

PubMed: 18611376
DOI: 10.1016/j.str.2008.04.009

実験手法

X-RAY DIFFRACTION (2.8 Å)