5mx9: Difference between revisions

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New page: '''Unreleased structure''' The entry 5mx9 is ON HOLD Authors: Hinchliffe, P., Coates, K., Walsh, T.R., Spencer, J. Description: High resolution crystal structure of the MCR-2 catalytic...
 
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'''Unreleased structure'''


The entry 5mx9 is ON HOLD
==High resolution crystal structure of the MCR-2 catalytic domain==
<StructureSection load='5mx9' size='340' side='right'caption='[[5mx9]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5mx9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MX9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MX9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.12&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=5mx9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5mx9 OCA], [https://pdbe.org/5mx9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5mx9 RCSB], [https://www.ebi.ac.uk/pdbsum/5mx9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5mx9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1C3NEV1_ECOLX A0A1C3NEV1_ECOLX]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MCR-2 confers resistance to colistin, a `last-line' antibiotic against extensively resistant Gram-negative pathogens. It is a plasmid-encoded phosphoethanolamine transferase that is closely related to MCR-1. To understand the diversity in the MCR family, the 1.12 A resolution crystal structure of the catalytic domain of MCR-2 was determined. Variable amino acids are located distant from both the di-zinc active site and the membrane-proximal face. The exceptionally high resolution will provide an accurate starting model for further mechanistic studies.


Authors: Hinchliffe, P., Coates, K., Walsh, T.R., Spencer, J.
1.12 A resolution crystal structure of the catalytic domain of the plasmid-mediated colistin resistance determinant MCR-2.,Coates K, Walsh TR, Spencer J, Hinchliffe P Acta Crystallogr F Struct Biol Commun. 2017 Aug 1;73(Pt 8):443-449. doi:, 10.1107/S2053230X17009669. Epub 2017 Jul 26. PMID:28777086<ref>PMID:28777086</ref>


Description: High resolution crystal structure of the MCR-2 catalytic domain
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Spencer, J]]
<div class="pdbe-citations 5mx9" style="background-color:#fffaf0;"></div>
[[Category: Coates, K]]
== References ==
[[Category: Walsh, T.R]]
<references/>
[[Category: Hinchliffe, P]]
__TOC__
</StructureSection>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Coates K]]
[[Category: Hinchliffe P]]
[[Category: Spencer J]]
[[Category: Walsh TR]]