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5tue

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Current revision (14:23, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5tue' size='340' side='right'caption='[[5tue]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
<StructureSection load='5tue' size='340' side='right'caption='[[5tue]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tue]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Uncultivated_bacterium Uncultivated bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TUE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TUE FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tue]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_bacterium Uncultured bacterium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TUE 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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 2.1&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tuf|5tuf]], [[5tui|5tui]], [[5tuk|5tuk]], [[5tul|5tul]], [[5tum|5tum]]</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=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=5tue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tue OCA], [http://pdbe.org/5tue PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tue RCSB], [http://www.ebi.ac.uk/pdbsum/5tue PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tue 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=5tue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tue OCA], [https://pdbe.org/5tue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tue RCSB], [https://www.ebi.ac.uk/pdbsum/5tue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tue 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/TET50_UNKP TET50_UNKP] An FAD-requiring monooxygenase active on tetracycline antibiotic and some of its derivatives, which leads to their inactivation (PubMed:26097034). Expression in E.coli confers high resistance to tetracycline and oxytetracycline, does not confer resistance to minocycline or tigecycline. Degrades tetracycline and oxytetracycline; the reaction requires NADPH (PubMed:26097034). Degrades and confers resistance to chlortetracycline (PubMed:28481346).<ref>PMID:26097034</ref> <ref>PMID:28481346</ref>
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Although tetracyclines are an important class of antibiotics for use in agriculture and the clinic, their efficacy is threatened by increasing resistance. Resistance to tetracyclines can occur through efflux, ribosomal protection, or enzymatic inactivation. Surprisingly, tetracycline enzymatic inactivation has remained largely unexplored, despite providing the distinct advantage of antibiotic clearance. The tetracycline destructases are a recently discovered family of tetracycline-inactivating flavoenzymes from pathogens and soil metagenomes that have a high potential for broad dissemination. Here, we show that tetracycline destructases accommodate tetracycline-class antibiotics in diverse and novel orientations for catalysis, and antibiotic binding drives unprecedented structural dynamics facilitating tetracycline inactivation. We identify a key inhibitor binding mode that locks the flavin adenine dinucleotide cofactor in an inactive state, functionally rescuing tetracycline activity. Our results reveal the potential of a new tetracycline and tetracycline destructase inhibitor combination therapy strategy to overcome resistance by enzymatic inactivation and restore the use of an important class of antibiotics.
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Plasticity, dynamics, and inhibition of emerging tetracycline resistance enzymes.,Park J, Gasparrini AJ, Reck MR, Symister CT, Elliott JL, Vogel JP, Wencewicz TA, Dantas G, Tolia NH Nat Chem Biol. 2017 May 8. doi: 10.1038/nchembio.2376. PMID:28481346<ref>PMID:28481346</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 5tue" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Uncultivated bacterium]]
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[[Category: Uncultured bacterium]]
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[[Category: Park, J]]
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[[Category: Park J]]
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[[Category: Tolia, N H]]
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[[Category: Tolia NH]]
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[[Category: Fad-binding]]
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[[Category: Oxidoreductase]]
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[[Category: Oxidoreductase activity]]
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[[Category: Tetracycline-inactivating]]
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Current revision

Crystal structure of tetracycline destructase Tet(50)

PDB ID 5tue

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