3tdv

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Current revision (10:08, 1 March 2024) (edit) (undo)
 
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<StructureSection load='3tdv' size='340' side='right'caption='[[3tdv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='3tdv' size='340' side='right'caption='[[3tdv]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3tdv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_49573 Atcc 49573]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TDV FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3tdv]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_gallinarum Enterococcus gallinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TDV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TDV FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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]] 2.2&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3tdw|3tdw]]</div></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=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=3tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdv OCA], [https://pdbe.org/3tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tdv RCSB], [https://www.ebi.ac.uk/pdbsum/3tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdv ProSAT]</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=3tdv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tdv OCA], [https://pdbe.org/3tdv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tdv RCSB], [https://www.ebi.ac.uk/pdbsum/3tdv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tdv 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/P96762_ENTGA P96762_ENTGA]
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Contrary to the accepted dogma that ATP is the canonical phosphate donor in aminoglycoside kinases and protein kinases, it was recently demonstrated that all members of the bacterial APH(2") aminoglycoside kinase family are unique in their ability to utilize GTP as a cofactor for antibiotic modification. Here we describe the structural determinants for GTP recognition in these enzymes. The crystal structure of the GTP-dependent APH(2")-IIIa shows that although this enzyme has templates for both ATP and GTP binding superimposed on a single nucleotide specificity motif, access to the ATP-binding template is blocked by a bulky tyrosine residue. Substitution of this tyrosine by a smaller amino acid opens access to the ATP template. Similar GTP-binding templates are conserved in other bacterial aminoglycoside kinases, while in the structurally-related eukaryotic protein kinases this template is less conserved. The aminoglycoside kinases are important antibiotic resistance enzymes in bacteria, whose wide dissemination severely limits available therapeutic options, and the GTP-binding templates could be exploited as new, previously unexplored targets for inhibitors of these clinically important enzymes.
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Aminoglycoside-2" phosphotransferase-IIIa (APH(2")-IIIa) prefers GTP over ATP: Structural templates for nucleotide recognition in the bacterial aminoglycoside-2" kinases.,Smith CA, Toth M, Frase H, Byrnes LJ, Vakulenko SB J Biol Chem. 2012 Feb 24. PMID:22367198<ref>PMID:22367198</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 3tdv" 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: Atcc 49573]]
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[[Category: Enterococcus gallinarum]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Smith, C A]]
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[[Category: Smith CA]]
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[[Category: Vakulenko, S B]]
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[[Category: Vakulenko SB]]
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[[Category: Antibiotic resistance]]
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[[Category: Gentamicin]]
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[[Category: Kinase]]
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[[Category: Phosphoryl transfer]]
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[[Category: Transferase]]
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Current revision

Structure of the GDP complex of wild-type aminoglycoside 2'-phosphotransferase-IIIa

PDB ID 3tdv

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