8er1
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==X-ray crystal structure of Tet(X6)== | |
| + | <StructureSection load='8er1' size='340' side='right'caption='[[8er1]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8er1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chryseobacterium_oncorhynchi Chryseobacterium oncorhynchi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8ER1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8ER1 FirstGlance]. <br> | ||
| + | </td></tr><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> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8er1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8er1 OCA], [https://pdbe.org/8er1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8er1 RCSB], [https://www.ebi.ac.uk/pdbsum/8er1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8er1 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A316WTJ0_9FLAO A0A316WTJ0_9FLAO] An FAD-requiring monooxygenase active on some tetracycline antibiotic derivatives, which leads to their inactivation. Hydroxylates carbon 11a of tetracycline and some analogs.[HAMAP-Rule:MF_00845] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Inactivation of tetracycline antibiotics by tetracycline destructases (TDases) remains a clinical and agricultural threat. TDases can be classified as type 1 Tet(X)-like TDases and type 2 soil-derived TDases. Type 1 TDases are widely identified in clinical pathogens. A combination therapy of tetracycline and a TDase inhibitor is much needed to rescue the clinical efficacy of tetracyclines. Anhydrotetracycline is a pan-TDase inhibitor that inhibits both type 1 and type 2 TDases. Here, we present structural, biochemical, and phenotypic evidence that anhydrotetracycline binds in a substrate-like orientation and competitively inhibits the type 1 TDase Tet(X6) to rescue tetracycline antibiotic activity as a sacrificial substrate. Anhydrotetracycline interacting residues of Tet(X6) are conserved within type 1 TDases, indicating a conserved binding mode and mechanism of inhibition. This mode of binding and inhibition is distinct from anhydrotetracycline's inhibition of type 2 TDases. This study forms the framework for development of next-generation therapies to counteract enzymatic tetracycline resistance. | ||
| - | + | Structure of anhydrotetracycline-bound Tet(X6) reveals the mechanism for inhibition of type 1 tetracycline destructases.,Kumar H, Williford EE, Blake KS, Virgin-Downey B, Dantas G, Wencewicz TA, Tolia NH Commun Biol. 2023 Apr 17;6(1):423. doi: 10.1038/s42003-023-04792-4. PMID:37062778<ref>PMID:37062778</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8er1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chryseobacterium oncorhynchi]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Kumar H]] | ||
| + | [[Category: Tolia NH]] | ||
Revision as of 17:06, 26 April 2023
X-ray crystal structure of Tet(X6)
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