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==NMR solution Structure of the E.coli Outer Membrane Protein W==
<StructureSection load='2mhl' size='340' side='right'caption='[[2mhl]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2mhl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_str._K-12_substr._DH10B Escherichia coli str. K-12 substr. DH10B]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHL FirstGlance]. <br>
</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=2mhl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhl OCA], [https://pdbe.org/2mhl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhl RCSB], [https://www.ebi.ac.uk/pdbsum/2mhl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhl ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
The outer membrane proteins (Omps) are key factors for bacterial survival and virulence. Among the Omps that have been structurally characterized either by X-ray crystallography or by NMR in solution, the crystal structure of OmpW stands out because three of its four extracellular loops are well defined, whereas long extracellular loops in other E. coli Omps are disordered in the crystals as well as in NMR structures. OmpW thus presented an opportunity for a detailed comparison of the extracellular loops in a beta-barrel membrane protein structure in crystals and in noncrystalline milieus. Here, the polypeptide backbone conformation of OmpW in 30-Fos micelles was determined. Complete backbone NMR assignments were obtained and the loops were structurally characterized. In combination with the OmpW crystal structure, NMR line shape analyses, and 15N{1H}-NOE data, these results showed that intact regular secondary structures in the loops undergo slow hinge motions at the detergent-solvent interface.

NMR Polypeptide Backbone Conformation of the E. coli Outer Membrane Protein W.,Horst R, Stanczak P, Wuthrich K Structure. 2014 Jul 9. pii: S0969-2126(14)00176-2. doi:, 10.1016/j.str.2014.05.016. PMID:25017731<ref>PMID:25017731</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli str. K-12 substr. DH10B]]
[[Category: Large Structures]]
[[Category: Horst R]]
[[Category: Stanczak P]]
[[Category: Wuthrich K]]