5tul

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Current revision (14:23, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5tul' size='340' side='right'caption='[[5tul]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='5tul' size='340' side='right'caption='[[5tul]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tul]] is a 1 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=5TUL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TUL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tul]] is a 1 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=5TUL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TUL 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=PO4:PHOSPHATE+ION'>PO4</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&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5tue|5tue]], [[5tuf|5tuf]], [[5tui|5tui]], [[5tuk|5tuk]], [[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=PO4:PHOSPHATE+ION'>PO4</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=5tul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tul OCA], [http://pdbe.org/5tul PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tul RCSB], [http://www.ebi.ac.uk/pdbsum/5tul PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tul 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=5tul FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tul OCA], [https://pdbe.org/5tul PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tul RCSB], [https://www.ebi.ac.uk/pdbsum/5tul PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tul 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/TET55_UNKP TET55_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 oxytetracycline, slightly less resistance to tetracycline, moderate resistance to minocycline but no resistance to 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 5tul" 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(55)

PDB ID 5tul

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OCA

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