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== | ==Outer Membrane Protein G== | ||
<StructureSection load='2jqy' size='340' side='right'caption='[[2jqy]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2jqy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JQY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JQY FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2jqy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jqy OCA], [https://pdbe.org/2jqy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jqy RCSB], [https://www.ebi.ac.uk/pdbsum/2jqy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jqy 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 == | |||
The bacterial outer membrane protein G (OmpG), a monomeric pH-gated porin, was overexpressed in Escherichia coli and refolded in beta-octyl glucoside micelles. After transfer into dodecylphosphocholine micelles, the solution structure of OmpG was determined by solution NMR spectroscopy at pH 6.3. 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. The global fold of the 14-stranded beta-barrel was determined based on 133 long-range NOEs observed between neighboring strands and local chemical shift and NOE information. The structure of the barrel is very similar to previous crystal structures, but the loops of the solution structure are quite flexible. | |||
Structure of outer membrane protein G by solution NMR spectroscopy.,Liang B, Tamm LK Proc Natl Acad Sci U S A. 2007 Oct 9;104(41):16140-5. Epub 2007 Oct 2. PMID:17911261<ref>PMID:17911261</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2jqy" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Porin 3D structures|Porin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Liang | [[Category: Liang B]] | ||
[[Category: Tamm | [[Category: Tamm LK]] | ||
Latest revision as of 19:39, 13 December 2023
Outer Membrane Protein GOuter Membrane Protein G
Structural highlights
FunctionOMPG_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 PubMedThe bacterial outer membrane protein G (OmpG), a monomeric pH-gated porin, was overexpressed in Escherichia coli and refolded in beta-octyl glucoside micelles. After transfer into dodecylphosphocholine micelles, the solution structure of OmpG was determined by solution NMR spectroscopy at pH 6.3. 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. The global fold of the 14-stranded beta-barrel was determined based on 133 long-range NOEs observed between neighboring strands and local chemical shift and NOE information. The structure of the barrel is very similar to previous crystal structures, but the loops of the solution structure are quite flexible. Structure of outer membrane protein G by solution NMR spectroscopy.,Liang B, Tamm LK Proc Natl Acad Sci U S A. 2007 Oct 9;104(41):16140-5. Epub 2007 Oct 2. PMID:17911261[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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