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==Refined structure of outer membrane protein x in nanodisc by measuring residual dipolar couplings==
==Refined structure of outer membrane protein x in nanodisc by measuring residual dipolar couplings==
<StructureSection load='2mnh' size='340' side='right'caption='[[2mnh]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
<StructureSection load='2mnh' size='340' side='right'caption='[[2mnh]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mnh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._k-12_substr._mc4100 Escherichia coli str. k-12 substr. mc4100]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MNH FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mnh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._MC4100 Escherichia coli str. K-12 substr. MC4100]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MNH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MNH FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B0814, BN896_0667, JW0799, ompX, YBIG ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1403831 Escherichia coli str. K-12 substr. MC4100])</td></tr>
</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=2mnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnh OCA], [https://pdbe.org/2mnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mnh RCSB], [https://www.ebi.ac.uk/pdbsum/2mnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mnh 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=2mnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mnh OCA], [https://pdbe.org/2mnh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mnh RCSB], [https://www.ebi.ac.uk/pdbsum/2mnh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mnh ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/OMPX_ECOLI OMPX_ECOLI]
Membrane proteins are involved in numerous vital biological processes. To understand membrane protein functionality, accurate structural information is required. Usually, structure determination and dynamics of membrane proteins are studied in micelles using either solution state NMR or X-ray crystallography. Even though invaluable information has been obtained by this approach, micelles are known to be far from ideal mimics of biological membranes often causing the loss or decrease of membrane protein activity. Recently, nanodiscs, which are composed of a lipid bilayer surrounded by apolipoproteins, have been introduced as a more physiological alternative than micelles for NMR investigations on membrane proteins. Here, we show that membrane protein bond orientations in nanodiscs can be obtained by measuring residual dipolar couplings (RDCs) with the outer membrane protein OmpX embedded in nanodiscs using Pf1 phage as an alignment medium. The presented collection of membrane protein RDCs in nanodiscs represents an important step toward more comprehensive structural and dynamical NMR-based investigations of membrane proteins in a natural bilayer environment.
 
Measuring membrane protein bond orientations in nanodiscs via residual dipolar couplings.,Bibow S, Carneiro MG, Sabo TM, Schwiegk C, Becker S, Riek R, Lee D Protein Sci. 2014 Jul;23(7):851-6. doi: 10.1002/pro.2482. Epub 2014 May 6. PMID:24752984<ref>PMID:24752984</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2mnh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Escherichia coli str. k-12 substr. mc4100]]
[[Category: Escherichia coli str. K-12 substr. MC4100]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Becker, S]]
[[Category: Becker S]]
[[Category: Bibow, S]]
[[Category: Bibow S]]
[[Category: Carneiro, M G]]
[[Category: Carneiro MG]]
[[Category: Lee, D]]
[[Category: Lee D]]
[[Category: Riek, R]]
[[Category: Riek R]]
[[Category: Sabo, T M]]
[[Category: Sabo TM]]
[[Category: Schwiegk, C]]
[[Category: Schwiegk C]]
[[Category: Beta barrel]]
[[Category: Membrane protein]]
[[Category: Nanodisc]]
[[Category: Ompx]]
[[Category: Residual dipolar coupling]]

Latest revision as of 07:01, 1 May 2024

Refined structure of outer membrane protein x in nanodisc by measuring residual dipolar couplings

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