2iwv | pdb_00002iwv

STRUCTURE OF THE MONOMERIC OUTER MEMBRANE PORIN OMPG IN THE OPEN AND CLOSED CONFORMATION

spinqualitylabelsall models 2iwv, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2iwv is a 4 chain structure with sequence from Ecoli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, LDA, TAM Related: 2f1c, 2iww Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed 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. Structure of the monomeric outer-membrane porin OmpG in the open and closed conformation.,Yildiz O, Vinothkumar KR, Goswami P, Kuhlbrandt W EMBO J. 2006 Aug 9;25(15):3702-13. Epub 2006 Aug 3. PMID:16888630 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Porin

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