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5mx9
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==High resolution crystal structure of the MCR-2 catalytic domain== | |
| + | <StructureSection load='5mx9' size='340' side='right'caption='[[5mx9]], [[Resolution|resolution]] 1.12Å' 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]] 1.12Å</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. | ||
| - | + | 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> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 5mx9" style="background-color:#fffaf0;"></div> |
| - | [[Category: Coates | + | == References == |
| - | [[Category: | + | <references/> |
| - | [[Category: | + | __TOC__ |
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Coates K]] | ||
| + | [[Category: Hinchliffe P]] | ||
| + | [[Category: Spencer J]] | ||
| + | [[Category: Walsh TR]] | ||
Current revision
High resolution crystal structure of the MCR-2 catalytic domain
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