3p9u: Difference between revisions

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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=3p9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p9u OCA], [https://pdbe.org/3p9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p9u RCSB], [https://www.ebi.ac.uk/pdbsum/3p9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p9u ProSAT]</span></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=3p9u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3p9u OCA], [https://pdbe.org/3p9u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3p9u RCSB], [https://www.ebi.ac.uk/pdbsum/3p9u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3p9u ProSAT]</span></td></tr>
</table>
</table>
== Function ==
<div style="background-color:#fffaf0;">
[https://www.uniprot.org/uniprot/TETX_BACT4 TETX_BACT4] An FAD-requiring monooxygenase active on tetracycline antibiotic derivatives, which leads to their inactivation (PubMed:15452119, PubMed:16128584). Hydroxylates carbon 11a of oxytetracycline and tigecycline (PubMed:15452119, PubMed:26097034). Acts on many tetracycline analogs (chlorotetracycline, demeclocycline, doxycycline, minocycline, oxytetracyclinee), probably by monooxygenization (PubMed:15452119, PubMed:16128584). Tigecycline, a new generation tetracycline antibiotic, is rendered less effective against E.coli by this monooxygenation, is much weaker at inhibiting translation in vitro and binds Mg(2+) considerably less well (PubMed:16128584, PubMed:26097034). Expression in E.coli BW25113 reduces its growth rate about 5%. The reaction probably proceeds by FAD reduction by NADPH and, second, hydroxylation of antibiotic in a ping-pong mechanism (PubMed:23236139). Degrades chlortetracycline, probably by monooxygenation (PubMed:15452119, PubMed:28481346). Slowly oxidizes anhydrotetracycline, the final substrate in tetracycline biosynthesis (PubMed:26097034).[HAMAP-Rule:MF_00845]<ref>PMID:15452119</ref> <ref>PMID:16128584</ref> <ref>PMID:23236139</ref> <ref>PMID:26097034</ref> <ref>PMID:28481346</ref>  
== Publication Abstract from PubMed ==
We have determined the structure of Bacteroides thetaiotaomicron TetX2 at 2.8 A resolution, and shown that it is a class A flavin dependent oxidoreductase. TetX2 has broad activity against a range of tetracyclines including one of the most recent tetracyclines, tigecycline (Tygacil((R))). Comparison of TetX2 with that of the weakly homologous Pseudomonas fluorescens para-hydroxybenzoate hydroxylase (PHBH) (21% identity) shows substantial differences among residues at the substrate binding site although FAD is positioned in a similar conformation between the two enzymes and is poised to carry out catalysis.
 
Crystal structure of Bacteroides thetaiotaomicron TetX2: a tetracycline degrading monooxygenase at 2.8 A resolution.,Walkiewicz K, Davlieva M, Wu G, Shamoo Y Proteins. 2011 Jul;79(7):2335-40. doi: 10.1002/prot.23052. Epub 2011 May 16. PMID:21590745<ref>PMID:21590745</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 3p9u" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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