View source for 5mwv


==Solid-state NMR Structure of outer membrane protein G in lipid bilayers==
<StructureSection load='5mwv' size='340' side='right'caption='[[5mwv]]' scene=''>
== Structural highlights ==
<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='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'>[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>
== 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> 
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== 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<ref>PMID:29233991</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5mwv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Large Structures]]
[[Category: Andreas LB]]
[[Category: Barbet-Massin E]]
[[Category: Bardiaux B]]
[[Category: Emsley L]]
[[Category: Franks WT]]
[[Category: Handel L]]
[[Category: Higman VA]]
[[Category: Hiller M]]
[[Category: Kuelbrandt W]]
[[Category: Nieuwkoop AJ]]
[[Category: Oschkinat H]]
[[Category: Pintacuda G]]
[[Category: Retel JS]]
[[Category: Stanek J]]
[[Category: Vinothkumar KR]]
[[Category: De Palma GG]]
[[Category: Van Rossum B-J]]