View source for 6bnc


==Crystal structure of the intrinsic colistin resistance enzyme ICR(Mc) from Moraxella catarrhalis, catalytic domain, Thr315Ala mutant di-zinc and PEG complex==
<StructureSection load='6bnc' size='340' side='right'caption='[[6bnc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bnc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Moraxella_sp._HMSC061H09 Moraxella sp. HMSC061H09]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BNC 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=15P:POLYETHYLENE+GLYCOL+(N=34)'>15P</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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=6bnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bnc OCA], [https://pdbe.org/6bnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bnc RCSB], [https://www.ebi.ac.uk/pdbsum/6bnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bnc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A1E9VP98_9GAMM A0A1E9VP98_9GAMM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Lipid A phosphoethanolamine (PEtN) transferases render bacteria resistant to the last resort antibiotic colistin. The recent discoveries of pathogenic bacteria harboring plasmid-borne PEtN transferase ( mcr) genes have illustrated the serious potential for wide dissemination of these resistance elements. The origin of mcr-1 is traced to Moraxella species co-occupying environmental niches with Enterobacteriaceae. Here, we describe the crystal structure of the catalytic domain of the chromosomally encoded colistin resistance PEtN transferase, ICR (Mc) (for intrinsic colistin resistance) of Moraxella catarrhalis. The ICR (Mc) structure in complex with PEtN reveals key molecular details including specific residues involved in catalysis and PEtN binding. It also demonstrates that ICR (Mc) catalytic domain dimerization is required for substrate binding. Our structure-guided phylogenetic analysis provides sequence signatures defining potentially colistin-active representatives in this enzyme family. Combined, these results advance the molecular and mechanistic understanding of PEtN transferases and illuminate their origins.

Substrate Recognition by a Colistin Resistance Enzyme from Moraxella catarrhalis.,Stogios PJ, Cox G, Zubyk HL, Evdokimova E, Wawrzak Z, Wright GD, Savchenko A ACS Chem Biol. 2018 Apr 19. doi: 10.1021/acschembio.8b00116. PMID:29631403<ref>PMID:29631403</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bnc" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Moraxella sp. HMSC061H09]]
[[Category: Anderson WF]]
[[Category: Evdokimova E]]
[[Category: Joachimiak A]]
[[Category: Satchell KJ]]
[[Category: Savchenko A]]
[[Category: Stogios PJ]]
[[Category: Wawrzak Z]]