6bbz
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bbz OCA], [http://pdbe.org/6bbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bbz RCSB], [http://www.ebi.ac.uk/pdbsum/6bbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bbz ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6bbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bbz OCA], [http://pdbe.org/6bbz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6bbz RCSB], [http://www.ebi.ac.uk/pdbsum/6bbz PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6bbz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 6bbz" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:49, 12 September 2018
Room temperature neutron/X-ray structure of sisomicin bound AAC-VIa
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