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6mb6

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Current revision (14:42, 13 March 2024) (edit) (undo)
 
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==AAC-IIIb binary with CoASH==
==AAC-IIIb binary with CoASH==
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<StructureSection load='6mb6' size='340' side='right' caption='[[6mb6]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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<StructureSection load='6mb6' size='340' side='right'caption='[[6mb6]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6mb6]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_aeruginosus"_(schroeter_1872)_trevisan_1885 "bacillus aeruginosus" (schroeter 1872) trevisan 1885]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MB6 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MB6 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6mb6]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MB6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6MB6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.25&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">aac(3)-IIIb ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 "Bacillus aeruginosus" (Schroeter 1872) Trevisan 1885])</td></tr>
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<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=MLI:MALONATE+ION'>MLI</scene></td></tr>
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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=6mb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mb6 OCA], [http://pdbe.org/6mb6 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6mb6 RCSB], [http://www.ebi.ac.uk/pdbsum/6mb6 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6mb6 ProSAT]</span></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=6mb6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6mb6 OCA], [https://pdbe.org/6mb6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6mb6 RCSB], [https://www.ebi.ac.uk/pdbsum/6mb6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6mb6 ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q51405_PSEAI Q51405_PSEAI]
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Aminoglycoside antibiotics are a large family of antibiotics that can be divided into two distinct classes on the basis of the substitution pattern of the central deoxystreptamine ring. Although aminoglycosides are chemically, structurally, and topologically diverse, some aminoglycoside-modifying enzymes (AGMEs) are able to inactivate as many as 15 aminoglycosides from the two main classes, the kanamycin- and neomycin-based antibiotics. Here, we present the crystal structure of a promiscuous AGME, aminoglycoside- N3-acetyltransferase-IIIb (AAC-IIIb), in the apo form, in binary drug (sisomicin, neomycin, and paromomycin) and coenzyme A (CoASH) complexes, and in the ternary neomycin-CoASH complex. These data provide a structural framework for interpretation of the thermodynamics of enzyme-ligand interactions and the role of solvent in the recognition of ligands. In combination with the recent structure of an AGME that does not have broad substrate specificity, these structures allow for the direct determination of how antibiotic promiscuity is encoded in some AGMEs.
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Encoding of Promiscuity in an Aminoglycoside Acetyltransferase.,Kumar P, Selvaraj B, Serpersu EH, Cuneo MJ J Med Chem. 2018 Oct 31. doi: 10.1021/acs.jmedchem.8b01393. PMID:30347146<ref>PMID:30347146</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6mb6" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Cuneo, M J]]
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[[Category: Large Structures]]
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[[Category: Kumar, P]]
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[[Category: Pseudomonas aeruginosa]]
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[[Category: Acetyltransferase]]
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[[Category: Cuneo MJ]]
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[[Category: Antibiotic resistance]]
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[[Category: Kumar P]]
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[[Category: Gnat]]
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[[Category: Promiscuity]]
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[[Category: Transferase]]
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Current revision

AAC-IIIb binary with CoASH

PDB ID 6mb6

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