2iwv
From Proteopedia
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- | {{Seed}} | ||
- | [[Image:2iwv.png|left|200px]] | ||
- | < | + | ==Structure of the monomeric outer membrane porin OmpG in the open and closed conformation== |
- | + | <StructureSection load='2iwv' size='340' side='right'caption='[[2iwv]], [[Resolution|resolution]] 2.30Å' scene=''> | |
- | + | == Structural highlights == | |
- | + | <table><tr><td colspan='2'>[[2iwv]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2IWV FirstGlance]. <br> | |
- | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> | |
- | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=TAM:TRIS(HYDROXYETHYL)AMINOMETHANE'>TAM</scene></td></tr> | |
- | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2iwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2iwv OCA], [https://pdbe.org/2iwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2iwv RCSB], [https://www.ebi.ac.uk/pdbsum/2iwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2iwv ProSAT]</span></td></tr> | |
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/OMPG_ECOLI OMPG_ECOLI] Forms channels functionally larger than those of classical porins.<ref>PMID:11758943</ref> May act as a regulator of the RCS-phosphorelay signal transduction pathway.<ref>PMID:11758943</ref> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == 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<ref>PMID:16888630</ref> | |
+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 2iwv" style="background-color:#fffaf0;"></div> | ||
- | + | ==See Also== | |
- | + | *[[Porin 3D structures|Porin 3D structures]] | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
- | == | + | [[Category: Escherichia coli K-12]] |
- | + | [[Category: Large Structures]] | |
- | + | [[Category: Goswami P]] | |
- | == | + | [[Category: Kuehlbrandt W]] |
- | < | + | [[Category: Vinothkumar KR]] |
- | [[Category: Escherichia coli | + | [[Category: Yildiz O]] |
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Current revision
Structure of the monomeric outer membrane porin OmpG in the open and closed conformation
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