3SYS

Improved crystal structure of Pseudomonas aeruginosa OccK1 (OpdK)

3SYS の概要

• エントリーDOI: 10.2210/pdb3sys/pdb
• 関連するPDBエントリー: 3SY7 3SY9 3SYB 3SZD 3SZV 3T0S 3T20 3T24
• 分子名称: Vanillate porin OpdK, 1,2-ETHANEDIOL, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (5 entities in total)
• 機能のキーワード: beta-barrel, channel, bacterial outer membrane, 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: 97676.52

構造登録者

van den Berg, B.,Eren, E. (登録日: 2011-07-18, 公開日: 2012-02-08, 最終更新日: 2023-09-13)

主引用文献

Eren, E.,Vijayaraghavan, J.,Liu, J.,Cheneke, B.R.,Touw, D.S.,Lepore, B.W.,Indic, M.,Movileanu, L.,van den Berg, B.
Substrate Specificity within a Family of Outer Membrane Carboxylate Channels.
Plos Biol., 10:e1001242-e1001242, 2012

PubMed Abstract: Many Gram-negative bacteria, including human pathogens such as Pseudomonas aeruginosa, do not have large-channel porins. This results in an outer membrane (OM) that is highly impermeable to small polar molecules, making the bacteria intrinsically resistant towards many antibiotics. In such microorganisms, the majority of small molecules are taken up by members of the OprD outer membrane protein family. Here we show that OprD channels require a carboxyl group in the substrate for efficient transport, and based on this we have renamed the family Occ, for outer membrane carboxylate channels. We further show that Occ channels can be divided into two subfamilies, based on their very different substrate specificities. Our results rationalize how certain bacteria can efficiently take up a variety of substrates under nutrient-poor conditions without compromising membrane permeability. In addition, they explain how channel inactivation in response to antibiotics can cause resistance but does not lead to decreased fitness.

PubMed: 22272184
DOI: 10.1371/journal.pbio.1001242

実験手法

X-RAY DIFFRACTION (1.65 Å)