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| | <StructureSection load='2x9k' size='340' side='right'caption='[[2x9k]], [[Resolution|resolution]] 2.18Å' scene=''> | | <StructureSection load='2x9k' size='340' side='right'caption='[[2x9k]], [[Resolution|resolution]] 2.18Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2x9k]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2X9K FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2x9k]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X9K OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X9K FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BOG:B-OCTYLGLUCOSIDE'>BOG</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2wvp|2wvp]], [[2f1c|2f1c]], [[2iww|2iww]], [[2iwv|2iwv]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2wvp|2wvp]], [[2f1c|2f1c]], [[2iww|2iww]], [[2iwv|2iwv]]</div></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2x9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9k OCA], [http://pdbe.org/2x9k PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2x9k RCSB], [http://www.ebi.ac.uk/pdbsum/2x9k PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9k ProSAT]</span></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=2x9k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x9k OCA], [https://pdbe.org/2x9k PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x9k RCSB], [https://www.ebi.ac.uk/pdbsum/2x9k PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x9k ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [[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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Structural highlights
Function
[OMPG_ECOLI] Forms channels functionally larger than those of classical porins.[1] May act as a regulator of the RCS-phosphorelay signal transduction pathway.[2]
Publication Abstract from PubMed
The channel activity of the outer-membrane protein G (OmpG) from Escherichia coli is pH-dependent. To investigate the role of the histidine pair His231/His261 in triggering channel opening and closing, we mutated both histidines to alanines and cysteines. Fourier transform infrared spectra revealed that the OmpG mutants stay-independent of pH-in an open conformation. Temperature ramp experiments indicate that the mutants are as stable as the open state of wild-type OmpG. The X-ray structure of the alanine-substituted OmpG mutant obtained at pH 6.5 confirms the constitutively open conformation. Compared to previous structures of the wild-type protein in the open and closed conformation, the mutant structure shows a difference in the extracellular loop L6 connecting beta-strands S12 and S13. A deletion of amino acids 220-228, which are thought to block the channel at low pH in wild-type OmpG, indicates conformational changes, which might be triggered by His231/His261.
Correlation between the OmpG secondary structure and its pH-dependent alterations monitored by FTIR.,Korkmaz-Ozkan F, Koster S, Kuhlbrandt W, Mantele W, Yildiz O J Mol Biol. 2010 Aug 6;401(1):56-67. Epub 2010 Jun 16. PMID:20561532[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
- ↑ Chen MH, Takeda S, Yamada H, Ishii Y, Yamashino T, Mizuno T. Characterization of the RcsC-->YojN-->RcsB phosphorelay signaling pathway involved in capsular synthesis in Escherichia coli. Biosci Biotechnol Biochem. 2001 Oct;65(10):2364-7. PMID:11758943
- ↑ Korkmaz-Ozkan F, Koster S, Kuhlbrandt W, Mantele W, Yildiz O. Correlation between the OmpG secondary structure and its pH-dependent alterations monitored by FTIR. J Mol Biol. 2010 Aug 6;401(1):56-67. Epub 2010 Jun 16. PMID:20561532 doi:10.1016/j.jmb.2010.06.015
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