5tum

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Current revision (14:23, 6 March 2024) (edit) (undo)
 
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<StructureSection load='5tum' size='340' side='right'caption='[[5tum]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
<StructureSection load='5tum' size='340' side='right'caption='[[5tum]], [[Resolution|resolution]] 3.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5tum]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33462 Atcc 33462]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TUM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5TUM FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5tum]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Legionella_longbeachae Legionella longbeachae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5TUM OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5TUM 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></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]] 3.299&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LLO_2673 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=450 ATCC 33462])</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></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=5tum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tum OCA], [http://pdbe.org/5tum PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5tum RCSB], [http://www.ebi.ac.uk/pdbsum/5tum PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5tum 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=5tum FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5tum OCA], [https://pdbe.org/5tum PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5tum RCSB], [https://www.ebi.ac.uk/pdbsum/5tum PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5tum 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/TET56_LEGLN TET56_LEGLN] 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. The reaction requires NADPH (PubMed:26097034). Expression in L.pneumophila confers resistance to tetracycline (PubMed:28481346). Degrades and confers resistance to tetracycline and chlortetracycline (PubMed:26097034, 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 5tum" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 33462]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Park, J]]
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[[Category: Legionella longbeachae]]
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[[Category: Tolia, N H]]
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[[Category: Park J]]
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[[Category: Fad-binding]]
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[[Category: Tolia NH]]
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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(56)

PDB ID 5tum

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Proteopedia Page Contributors and Editors (what is this?)

OCA

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