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2f1c

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Crystal structure of the monomeric porin OmpG

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Categories: Escherichia coli K-12 | Large Structures | Subbarao GV | Van den Berg B

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 <StructureSection load='2f1c' size='340' side='right'caption='[[2f1c]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2f1c]] 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=2F1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F1C FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2f1c]] is a 1 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=2F1C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F1C FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ompG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</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=2f1c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f1c OCA], [https://pdbe.org/2f1c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f1c RCSB], [https://www.ebi.ac.uk/pdbsum/2f1c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f1c 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>
+[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 outer membrane (OM) of Gram-negative bacteria contains a large number of channel proteins that mediate the uptake of ions and nutrients necessary for growth and functioning of the cell. An important group of OM channel proteins are the porins, which mediate the non-specific, diffusion-based passage of small (&lt;600 Da) polar molecules. All porins of Gram-negative bacteria that have been crystallized to date form stable trimers, with each monomer composed of a 16-stranded beta-barrel with a relatively narrow central pore. In contrast, the OmpG porin is unique, as it appears to function as a monomer. We have determined the X-ray crystal structure of OmpG from Escherichia coli to a resolution of 2.3 A. The structure shows a 14-stranded beta-barrel with a relatively simple architecture. Due to the absence of loops that fold back into the channel, OmpG has a large ( approximately 13 A) central pore that is considerably wider than those of other E. coli porins, and very similar in size to that of the toxin alpha-hemolysin. The architecture of the channel, together with previous biochemical and other data, suggests that OmpG may form a non-specific channel for the transport of larger oligosaccharides. The structure of OmpG provides the starting point for engineering studies aiming to generate selective channels and for the development of biosensors.
-Crystal structure of the monomeric porin OmpG.,Subbarao GV, van den Berg B J Mol Biol. 2006 Jul 21;360(4):750-9. Epub 2006 Jun 2. PMID:16797588<ref>PMID:16797588</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 2f1c" style="background-color:#fffaf0;"></div>
 ==See Also==
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 __TOC__
 </StructureSection>
-[[Category: Ecoli]]
+[[Category: Escherichia coli K-12]]
 [[Category: Large Structures]]
-[[Category: Berg, B van den]]
+[[Category: Subbarao GV]]
-[[Category: Subbarao, G V]]
+[[Category: Van den Berg B]]
-[[Category: Beta barrel]]
-[[Category: Membrane protein]]

2f1c

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Crystal structure of the monomeric porin OmpG

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