2IWW
Structure of the monomeric outer membrane porin OmpG in the open and closed conformation
Summary for 2IWW
| Entry DOI | 10.2210/pdb2iww/pdb |
| Related | 2F1C 2IWV |
| Descriptor | OUTER MEMBRANE PROTEIN G, beta-D-glucopyranose, LAURYL DIMETHYLAMINE-N-OXIDE, ... (5 entities in total) |
| Functional Keywords | transmembrane, outer membrane, ion channel, porin, membrane, transport, ion transport |
| Biological source | ESCHERICHIA COLI |
| Cellular location | Cell outer membrane; Multi-pass membrane protein: P76045 |
| Total number of polymer chains | 2 |
| Total formula weight | 70331.51 |
| Authors | Yildiz, O.,Vinothkumar, K.R.,Goswami, P.,Kuehlbrandt, W. (deposition date: 2006-07-05, release date: 2006-08-14, Last modification date: 2024-05-08) |
| Primary citation | 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 Cited by 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: 16888630DOI: 10.1038/SJ.EMBOJ.7601237 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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