2X9K

Structure of a E.coli porin

2X9K の概要

• エントリーDOI: 10.2210/pdb2x9k/pdb
• 関連するPDBエントリー: 2F1C 2IWV 2IWW 2WVP
• 分子名称: OUTER MEMBRANE PROTEIN G, octyl beta-D-glucopyranoside (3 entities in total)
• 機能のキーワード: transport protein, ion transport
• 由来する生物種: ESCHERICHIA COLI
• 細胞内の位置: Cell outer membrane; Multi-pass membrane protein: P76045
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 35302.52

構造登録者

Korkmaz-Ozkan, F.,Koster, S.,Kuhlbrandt, W.,Mantele, W.,Yildiz, O. (登録日: 2010-03-21, 公開日: 2011-01-26, 最終更新日: 2024-05-08)

主引用文献

Korkmaz-Ozkan, F.,Koster, S.,Kuhlbrandt, W.,Mantele, W.,Yildiz, O.
Correlation between the Ompg Secondary Structure and its Ph-Dependent Alterations Monitored by Ftir.
J.Mol.Biol., 401:56-, 2010

PubMed Abstract: The channel activity of the outer-membrane protein G (OmpG) from Escherichia coli is pH-dependent. To investigate the role of the histidine pair His231/His261 in triggering channel opening and closing, we mutated both histidines to alanines and cysteines. Fourier transform infrared spectra revealed that the OmpG mutants stay-independent of pH-in an open conformation. Temperature ramp experiments indicate that the mutants are as stable as the open state of wild-type OmpG. The X-ray structure of the alanine-substituted OmpG mutant obtained at pH 6.5 confirms the constitutively open conformation. Compared to previous structures of the wild-type protein in the open and closed conformation, the mutant structure shows a difference in the extracellular loop L6 connecting beta-strands S12 and S13. A deletion of amino acids 220-228, which are thought to block the channel at low pH in wild-type OmpG, indicates conformational changes, which might be triggered by His231/His261.

PubMed: 20561532
DOI: 10.1016/J.JMB.2010.06.015

実験手法

X-RAY DIFFRACTION (2.18 Å)