View source for 6bc3


==Cryo X-ray structure of sisomicin bound AAC-VIa==
<StructureSection load='6bc3' size='340' side='right'caption='[[6bc3]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6bc3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BC3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BC3 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]] 2.047&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=SIS:(1S,2S,3R,4S,6R)-4,6-DIAMINO-3-{[(2S,3R)-3-AMINO-6-(AMINOMETHYL)-3,4-DIHYDRO-2H-PYRAN-2-YL]OXY}-2-HYDROXYCYCLOHEXYL+3-DEOXY-4-C-METHYL-3-(METHYLAMINO)-BETA-L-ARABINOPYRANOSIDE'>SIS</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=6bc3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bc3 OCA], [https://pdbe.org/6bc3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bc3 RCSB], [https://www.ebi.ac.uk/pdbsum/6bc3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bc3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q47030_ENTCL Q47030_ENTCL] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
One group of enzymes that confer resistance to aminoglycoside antibiotics through covalent modification belongs to the GCN5-related N-acetyltransferase (GNAT) superfamily. We show how a unique GNAT subfamily member uses a previously unidentified noncanonical catalytic triad, consisting of a glutamic acid, a histidine, and the antibiotic substrate itself, which acts as a nucleophile and attacks the acetyl donor molecule. Neutron diffraction studies allow for unambiguous identification of a low-barrier hydrogen bond, predicted in canonical catalytic triads to increase basicity of the histidine. This work highlights the role of this unique catalytic triad in mediating antibiotic resistance while providing new insights into the design of the next generation of aminoglycosides.

A low-barrier hydrogen bond mediates antibiotic resistance in a noncanonical catalytic triad.,Kumar P, Serpersu EH, Cuneo MJ Sci Adv. 2018 Apr 4;4(4):eaas8667. doi: 10.1126/sciadv.aas8667. eCollection 2018 , Apr. PMID:29632894<ref>PMID:29632894</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6bc3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Enterobacter cloacae]]
[[Category: Large Structures]]
[[Category: Cuneo MJ]]
[[Category: Kumar P]]
[[Category: Serpersu EH]]