2n2m: Difference between revisions

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New page: '''Unreleased structure''' The entry 2n2m is ON HOLD Authors: Marassi, F.M., Ding, Y., Yao, Y. Description: NMR structure of yersinia pestis Ail (attachment invasion locus) in decylpho...
 
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'''Unreleased structure'''


The entry 2n2m is ON HOLD
==NMR structure of yersinia pestis Ail (attachment invasion locus) in decylphosphocholine micelles==
<StructureSection load='2n2m' size='340' side='right'caption='[[2n2m]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2n2m]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Yersinia_pestis Yersinia pestis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2N2M OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2N2M 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=2n2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2n2m OCA], [https://pdbe.org/2n2m PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2n2m RCSB], [https://www.ebi.ac.uk/pdbsum/2n2m PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2n2m ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8D0Z7_YERPE Q8D0Z7_YERPE]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The outer membrane protein Ail (attachment invasion locus) is a virulence factor of Yersinia pestis that mediates cell invasion, cell attachment and complement resistance. Here we describe its three-dimensional backbone structure determined in decyl-phosphocholine (DePC) micelles by NMR spectroscopy. The NMR structure was calculated using the membrane function of the implicit solvation potential, eefxPot, which we have developed to facilitate NMR structure calculations in a physically realistic environment. We show that the eefxPot force field guides the protein towards its native fold. The resulting structures provide information about the membrane-embedded global position of Ail, and have higher accuracy, higher precision and improved conformational properties, compared to the structures calculated with the standard repulsive potential.


Authors: Marassi, F.M., Ding, Y., Yao, Y.
Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation.,Marassi FM, Ding Y, Schwieters CD, Tian Y, Yao Y J Biomol NMR. 2015 Jul 5. PMID:26143069<ref>PMID:26143069</ref>


Description: NMR structure of yersinia pestis Ail (attachment invasion locus) in decylphosphocholine micelles
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Yao, Y]]
<div class="pdbe-citations 2n2m" style="background-color:#fffaf0;"></div>
[[Category: Marassi, F.M]]
== References ==
[[Category: Ding, Y]]
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Yersinia pestis]]
[[Category: Ding Y]]
[[Category: Marassi FM]]
[[Category: Yao Y]]

Latest revision as of 06:13, 15 May 2024

NMR structure of yersinia pestis Ail (attachment invasion locus) in decylphosphocholine micelles

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