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| | ==Solid-state NMR Structure of outer membrane protein G in lipid bilayers== | | ==Solid-state NMR Structure of outer membrane protein G in lipid bilayers== |
| - | <StructureSection load='5mwv' size='340' side='right'caption='[[5mwv]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='5mwv' size='340' side='right'caption='[[5mwv]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5mwv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MWV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5MWV FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5mwv]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MWV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MWV FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ompG, b1319, JW1312 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</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=5mwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mwv OCA], [http://pdbe.org/5mwv PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5mwv RCSB], [http://www.ebi.ac.uk/pdbsum/5mwv PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5mwv 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=5mwv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mwv OCA], [https://pdbe.org/5mwv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mwv RCSB], [https://www.ebi.ac.uk/pdbsum/5mwv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mwv 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 == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andreas, L B]] | + | [[Category: Andreas LB]] |
| - | [[Category: Barbet-Massin, E]] | + | [[Category: Barbet-Massin E]] |
| - | [[Category: Bardiaux, B]] | + | [[Category: Bardiaux B]] |
| - | [[Category: Emsley, L]] | + | [[Category: Emsley L]] |
| - | [[Category: Franks, W T]] | + | [[Category: Franks WT]] |
| - | [[Category: Handel, L]] | + | [[Category: Handel L]] |
| - | [[Category: Higman, V A]] | + | [[Category: Higman VA]] |
| - | [[Category: Hiller, M]] | + | [[Category: Hiller M]] |
| - | [[Category: Kuelbrandt, W]] | + | [[Category: Kuelbrandt W]] |
| - | [[Category: Nieuwkoop, A J]] | + | [[Category: Nieuwkoop AJ]] |
| - | [[Category: Oschkinat, H]] | + | [[Category: Oschkinat H]] |
| - | [[Category: Palma, G G.de]]
| + | [[Category: Pintacuda G]] |
| - | [[Category: Pintacuda, G]] | + | [[Category: Retel JS]] |
| - | [[Category: Retel, J S]] | + | [[Category: Stanek J]] |
| - | [[Category: Rossum, B J.van]]
| + | [[Category: Vinothkumar KR]] |
| - | [[Category: Stanek, J]] | + | [[Category: De Palma GG]] |
| - | [[Category: Vinothkumar, K R]] | + | [[Category: Van Rossum B-J]] |
| - | [[Category: Membrane protein]] | + | |
| - | [[Category: Porin beta-barrel membrane lipid]] | + | |
| 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
beta-barrel proteins mediate nutrient uptake in bacteria and serve vital functions in cell signaling and adhesion. For the 14-strand outer membrane protein G of Escherichia coli, opening and closing is pH-dependent. Different roles of the extracellular loops in this process were proposed, and X-ray and solution NMR studies were divergent. Here, we report the structure of outer membrane protein G investigated in bilayers of E. coli lipid extracts by magic-angle-spinning NMR. In total, 1847 inter-residue (1)H-(1)H and (13)C-(13)C distance restraints, 256 torsion angles, but no hydrogen bond restraints are used to calculate the structure. The length of beta-strands is found to vary beyond the membrane boundary, with strands 6-8 being the longest and the extracellular loops 3 and 4 well ordered. The site of barrel closure at strands 1 and 14 is more disordered than most remaining strands, with the flexibility decreasing toward loops 3 and 4. Loop 4 presents a well-defined helix.
Structure of outer membrane protein G in lipid bilayers.,Retel JS, Nieuwkoop AJ, Hiller M, Higman VA, Barbet-Massin E, Stanek J, Andreas LB, Franks WT, van Rossum BJ, Vinothkumar KR, Handel L, de Palma GG, Bardiaux B, Pintacuda G, Emsley L, Kuhlbrandt W, Oschkinat H Nat Commun. 2017 Dec 12;8(1):2073. doi: 10.1038/s41467-017-02228-2. PMID:29233991[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Retel JS, Nieuwkoop AJ, Hiller M, Higman VA, Barbet-Massin E, Stanek J, Andreas LB, Franks WT, van Rossum BJ, Vinothkumar KR, Handel L, de Palma GG, Bardiaux B, Pintacuda G, Emsley L, Kuhlbrandt W, Oschkinat H. Structure of outer membrane protein G in lipid bilayers. Nat Commun. 2017 Dec 12;8(1):2073. doi: 10.1038/s41467-017-02228-2. PMID:29233991 doi:http://dx.doi.org/10.1038/s41467-017-02228-2
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