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5byl

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==Aminoglycoside Phosphotransferase (2'')-Ia (CTD of AAC(6')-Ie/APH(2'')-Ia) in complex with GMPPCP and Magnesium==
==Aminoglycoside Phosphotransferase (2'')-Ia (CTD of AAC(6')-Ie/APH(2'')-Ia) in complex with GMPPCP and Magnesium==
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<StructureSection load='5byl' size='340' side='right' caption='[[5byl]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
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<StructureSection load='5byl' size='340' side='right'caption='[[5byl]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5byl]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BYL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5BYL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5byl]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5BYL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5BYL 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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]] 2.15&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5iqa|5iqa]], [[5iqb|5iqb]], [[5iqc|5iqc]], [[5iqd|5iqd]], [[5iqe|5iqe]], [[5iqf|5iqf]], [[5iqg|5iqg]], [[5iqh|5iqh]], [[5iqi|5iqi]]</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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GCP:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANYLATE+ESTER'>GCP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=5byl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5byl OCA], [http://pdbe.org/5byl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5byl RCSB], [http://www.ebi.ac.uk/pdbsum/5byl PDBsum]</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=5byl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5byl OCA], [https://pdbe.org/5byl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5byl RCSB], [https://www.ebi.ac.uk/pdbsum/5byl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5byl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/AACA_STAAU AACA_STAAU]] Resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region, and the gentamicin resistance is due to the APH activity encoded by the C-terminal region of the protein.
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[https://www.uniprot.org/uniprot/AACA_STAAU AACA_STAAU] Resistance to gentamicin, tobramycin, and kanamycin. Tobramycin and kanamycin resistance is due to the ACC activity, specified by N-terminal region, and the gentamicin resistance is due to the APH activity encoded by the C-terminal region of the protein.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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APH(2'')-Ia is a widely disseminated resistance factor frequently found in clinical isolates of Staphylococcus aureus and pathogenic enterococci, where it is constitutively expressed. APH(2'')-Ia confers high-level resistance to gentamicin and related aminoglycosides through phosphorylation of the antibiotic using guanosine triphosphate (GTP) as phosphate donor. We have determined crystal structures of the APH(2'')-Ia in complex with GTP analogs, guanosine diphosphate, and aminoglycosides. These structures collectively demonstrate that aminoglycoside binding to the GTP-bound kinase drives conformational changes that bring distant regions of the protein into contact. These changes in turn drive a switch of the triphosphate cofactor from an inactive, stabilized conformation to a catalytically competent active conformation. This switch has not been previously reported for antibiotic kinases or for the structurally related eukaryotic protein kinases. This catalytic triphosphate switch presents a means by which the enzyme can curtail wasteful hydrolysis of GTP in the absence of aminoglycosides, providing an evolutionary advantage to this enzyme.
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Antibiotic Binding Drives Catalytic Activation of Aminoglycoside Kinase APH(2'')-Ia.,Caldwell SJ, Huang Y, Berghuis AM Structure. 2016 May 5. pii: S0969-2126(16)30038-7. doi:, 10.1016/j.str.2016.04.002. PMID:27161980<ref>PMID:27161980</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 5byl" 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: Berghuis, A M]]
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[[Category: Large Structures]]
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[[Category: Caldwell, S J]]
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[[Category: Staphylococcus aureus]]
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[[Category: Aminoglycoside]]
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[[Category: Berghuis AM]]
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[[Category: Antibiotic]]
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[[Category: Caldwell SJ]]
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[[Category: Kinase]]
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[[Category: Resistance]]
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[[Category: Transferase]]
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Current revision

Aminoglycoside Phosphotransferase (2)-Ia (CTD of AAC(6')-Ie/APH(2)-Ia) in complex with GMPPCP and Magnesium

PDB ID 5byl

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