5mwv: Difference between revisions
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The | ==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=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5mwv]] is a 1 chain structure. 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> | |||
</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> | |||
</table> | |||
== 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> | |||
<div style="background-color:#fffaf0;"> | |||
== 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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 5mwv" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
[[Category: | __TOC__ | ||
</StructureSection> | |||
[[Category: Andreas, L B]] | |||
[[Category: Barbet-Massin, E]] | [[Category: Barbet-Massin, E]] | ||
[[Category: Bardiaux, B]] | [[Category: Bardiaux, B]] | ||
[[Category: Nieuwkoop, A | [[Category: Emsley, L]] | ||
[[Category: | [[Category: Franks, W T]] | ||
[[Category: Handel, L]] | |||
[[Category: Higman, V A]] | |||
[[Category: Hiller, M]] | |||
[[Category: Kuelbrandt, W]] | |||
[[Category: Nieuwkoop, A J]] | |||
[[Category: Oschkinat, H]] | |||
[[Category: Palma, G G.de]] | |||
[[Category: Pintacuda, G]] | [[Category: Pintacuda, G]] | ||
[[Category: | [[Category: Retel, J S]] | ||
[[Category: Rossum, B J.van]] | |||
[[Category: | |||
[[Category: Stanek, J]] | [[Category: Stanek, J]] | ||
[[Category: | [[Category: Vinothkumar, K R]] | ||
[[Category: Membrane protein]] | |||
[[Category: Porin beta-barrel membrane lipid]] | |||
