2xdo: Difference between revisions
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New page: '''Unreleased structure''' The entry 2xdo is ON HOLD Authors: Volkers, G., Palm, G., Wright, G.D., Hinrichs, W. Description: Structure of the Tetracycline degrading Monooxygenase TetX2... |
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==Structure of the Tetracycline degrading Monooxygenase TetX2 from Bacteroides thetaiotaomicron== | |||
<StructureSection load='2xdo' size='340' side='right'caption='[[2xdo]], [[Resolution|resolution]] 2.09Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xdo]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_thetaiotaomicron Bacteroides thetaiotaomicron]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XDO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XDO FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.09Å</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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=2xdo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xdo OCA], [https://pdbe.org/2xdo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xdo RCSB], [https://www.ebi.ac.uk/pdbsum/2xdo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xdo ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[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> | |||
==See Also== | |||
*[[Monooxygenase 3D structures|Monooxygenase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bacteroides thetaiotaomicron]] | |||
[[Category: Large Structures]] | |||
[[Category: Hinrichs W]] | |||
[[Category: Palm GJ]] | |||
[[Category: Volkers G]] | |||
[[Category: Wright GD]] | |||
