7mql
From Proteopedia
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==AAC(3)-IIIa in complex with CoA and neomycin== | ==AAC(3)-IIIa in complex with CoA and neomycin== | ||
| - | <StructureSection load='7mql' size='340' side='right'caption='[[7mql]]' scene=''> | + | <StructureSection load='7mql' size='340' side='right'caption='[[7mql]], [[Resolution|resolution]] 1.60Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MQL FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7mql]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7MQL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7MQL FirstGlance]. <br> |
| - | </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=7mql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mql OCA], [https://pdbe.org/7mql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mql RCSB], [https://www.ebi.ac.uk/pdbsum/7mql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mql ProSAT]</span></td></tr> | + | </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=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=RIO:RIBOSTAMYCIN'>RIO</scene></td></tr> |
| + | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene></td></tr> | ||
| + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Aminoglycoside_N(3')-acetyltransferase Aminoglycoside N(3')-acetyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.81 2.3.1.81] </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=7mql FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7mql OCA], [https://pdbe.org/7mql PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7mql RCSB], [https://www.ebi.ac.uk/pdbsum/7mql PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7mql ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[https://www.uniprot.org/uniprot/AACC3_PSEAI AACC3_PSEAI]] Resistance to antibiotics containing the 2-deoxy-streptamine ring including dibekacin, gentamicin, kanamycin, sisomicin, tobramycin, neomycin and to a lesser extent netilmicin. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Canonical aminoglycosides are a large group of antibiotics, where the part of chemical diversity stems from the substitution of the neamine ring system on positions 5 and 6. Certain aminoglycoside modifying enzymes can modify a broad range of 4,5- and 4,6-disubstituted aminoglycosides, with some as many as 15. This study presents the structural and kinetic results describing a promiscuous aminoglycoside acetyltransferase AAC(3)-IIIa. This enzyme has been crystallized in ternary complex with coenzyme A and 4,5- and 4,6-disubstituted aminoglycosides. We have followed up this work with kinetic characterization utilizing a panel of diverse aminoglycosides, including a next-generation aminoglycoside, plazomicin. Lastly, we observed an alternative binding mode of gentamicin in the aminoglycoside binding site, which was proven to be a crystallographic artifact based on mutagenesis. | ||
| + | |||
| + | Structural elucidation of substrate-bound aminoglycoside acetyltransferase (3)-IIIa.,Zielinski M, Blanchet J, Hailemariam S, Berghuis AM PLoS One. 2022 Aug 3;17(8):e0269684. doi: 10.1371/journal.pone.0269684., eCollection 2022. PMID:35921328<ref>PMID:35921328</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7mql" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Berghuis | + | [[Category: Berghuis, A M]] |
| - | [[Category: Zielinski M]] | + | [[Category: Zielinski, M]] |
| + | [[Category: Acetyltransferase]] | ||
| + | [[Category: Aminoglycoside]] | ||
| + | [[Category: Antibiotic resistance]] | ||
| + | [[Category: Transferase]] | ||
Revision as of 06:34, 18 August 2022
AAC(3)-IIIa in complex with CoA and neomycin
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