5O77

Klebsiella pneumoniae OmpK35

5O77 の概要

• エントリーDOI: 10.2210/pdb5o77/pdb
• 分子名称: OmpK35, 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, ... (4 entities in total)
• 機能のキーワード: outer membrane protein, porin, ion transport, ompf ortholog, membrane protein
• 由来する生物種: Klebsiella pneumoniae
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 38179.42

構造登録者

van den berg, B.,Pathania, M.,Zahn, M. (登録日: 2017-06-08, 公開日: 2018-06-20, 最終更新日: 2024-01-17)

主引用文献

Acosta-Gutierrez, S.,Ferrara, L.,Pathania, M.,Masi, M.,Wang, J.,Bodrenko, I.,Zahn, M.,Winterhalter, M.,Stavenger, R.A.,Pages, J.M.,Naismith, J.H.,van den Berg, B.,Page, M.G.P.,Ceccarelli, M.
Getting Drugs into Gram-Negative Bacteria: Rational Rules for Permeation through General Porins.
Acs Infect Dis., 4:1487-1498, 2018

PubMed Abstract: Small, hydrophilic molecules, including most important antibiotics in clinical use, cross the Gram-negative outer membrane through the water-filled channels provided by porins. We have determined the X-ray crystal structures of the principal general porins from three species of Enterobacteriaceae, namely Enterobacter aerogenes, Enterobacter cloacae, and Klebsiella pneumoniae, and determined their antibiotic permeabilities as well as those of the orthologues from Escherichia coli. Starting from the structure of the porins and molecules, we propose a physical mechanism underlying transport and condense it in a computationally efficient scoring function. The scoring function shows good agreement with in vitro penetration data and will enable the screening of virtual databases to identify molecules with optimal permeability through porins and help to guide the optimization of antibiotics with poor permeation.

PubMed: 29962203
DOI: 10.1021/acsinfecdis.8b00108

実験手法

X-RAY DIFFRACTION (1.5 Å)