ompG Antibody

1. The X-ray structure of the alanine-substituted OmpG mutant obtained at pH 6.5 confirms the constitutively open conformation. PMID: 20561532
2. At acidic pH, the authors detected a pH-dependent interaction at loop L6. This interaction changed the (un)folding of loop L6 and of beta-strands 11 and 12, which connect loop L6. PMID: 20171227
3. Upon lowering the pH to 5.0, the conformation of OmpG molecules changed to close the extracellular entrance of their channel. PMID: 20036258
4. The architecture of the channel, together with previous biochemical and other data, suggests that OmpG may form a non-specific channel for the transport of larger oligosaccharides. PMID: 16797588
5. In the 2.7 A structure, OmpG binds one OG and one glucose molecule as sugar substrates in the closed pore. PMID: 16888630
6. Complete backbone assignments were obtained for 234 of 280 residues based on CA, CB, and CO connection pathways determined from a series of TROSY-based 3D experiments at 800 MHz. PMID: 17911261
7. Molecular dynamics simulations were used to identify regions of OmpG implicated in the gating. PMID: 18443290

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KEGG: ecj:JW1312

STRING: 316385.ECDH10B_1438