2IWV

Structure of the monomeric outer membrane porin OmpG in the open and closed conformation

2IWV の概要

• エントリーDOI: 10.2210/pdb2iwv/pdb
• 関連するPDBエントリー: 2F1C 2IWW
• 分子名称: OUTER MEMBRANE PROTEIN G, CALCIUM ION, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total)
• 機能のキーワード: transmembrane, outer membrane, ion channel, porin, membrane, transport, 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: 4
• 化学式量合計: 168101.00

構造登録者

Yildiz, O.,Vinothkumar, K.R.,Goswami, P.,Kuehlbrandt, W. (登録日: 2006-07-04, 公開日: 2006-08-14, 最終更新日: 2024-05-08)

主引用文献

Yildiz, O.,Vinothkumar, K.R.,Goswami, P.,Kuhlbrandt, W.
Structure of the Monomeric Outer-Membrane Porin Ompg in the Open and Closed Conformation.
Embo J., 25:3702-, 2006

PubMed Abstract: OmpG, a monomeric pore-forming protein from Escherichia coli outer membranes, was refolded from inclusion bodies and crystallized in two different conformations. The OmpG channel is a 14-stranded beta-barrel, with short periplasmic turns and seven extracellular loops. Crystals grown at neutral pH show the channel in the open state at 2.3 A resolution. In the 2.7 A structure of crystals grown at pH 5.6, the pore is blocked by loop 6, which folds across the channel. The rearrangement of loop 6 appears to be triggered by a pair of histidine residues, which repel one another at acidic pH, resulting in the breakage of neighbouring H-bonds and a lengthening of loop 6 from 10 to 17 residues. A total of 151 ordered LDAO detergent molecules were found in the 2.3 A structure, mostly on the hydrophobic outer surface of OmpG, mimicking the outer membrane lipid bilayer, with three LDAO molecules in the open pore. In the 2.7 A structure, OmpG binds one OG and one glucose molecule as sugar substrates in the closed pore.

PubMed: 16888630
DOI: 10.1038/SJ.EMBOJ.7601237

実験手法

X-RAY DIFFRACTION (2.3 Å)