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6sut
From Proteopedia
(Difference between revisions)
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| - | == | + | ==n/a== |
| - | <StructureSection load='6sut' size='340' side='right'caption='[[6sut]] | + | <StructureSection load='6sut' size='340' side='right'caption='[[6sut]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6SUT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6SUT FirstGlance]. <br> |
| - | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction</td></tr> |
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6sut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sut OCA], [https://pdbe.org/6sut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sut RCSB], [https://www.ebi.ac.uk/pdbsum/6sut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sut 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=6sut FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6sut OCA], [https://pdbe.org/6sut PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6sut RCSB], [https://www.ebi.ac.uk/pdbsum/6sut PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6sut ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/A0A1C3NEV1_ECOLX A0A1C3NEV1_ECOLX] | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | MCR (mobile colistin resistance) enzymes catalyse phosphoethanolamine (PEA) addition to bacterial lipid A, threatening the "last-resort" antibiotic colistin. Molecular dynamics and density functional theory simulations indicate that monozinc MCR supports PEA transfer to the Thr285 acceptor, positioning MCR as a mono- rather than multinuclear member of the alkaline phosphatase superfamily. | ||
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| - | Resistance to the "last resort" antibiotic colistin: a single-zinc mechanism for phosphointermediate formation in MCR enzymes.,Lythell E, Suardiaz R, Hinchliffe P, Hanpaibool C, Visitsatthawong S, Oliveira ASF, Lang EJM, Surawatanawong P, Lee VS, Rungrotmongkol T, Fey N, Spencer J, Mulholland AJ Chem Commun (Camb). 2020 Jun 23;56(50):6874-6877. doi: 10.1039/d0cc02520h. PMID:32432618<ref>PMID:32432618</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 6sut" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Escherichia coli]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: N/a]] |
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Current revision
n/a
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