5je0

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==Crystal structure of Burkholderia glumae ToxA with bound S-adenosylhomocysteine (SAH) and 1,6-didemethyltoxoflavin==
==Crystal structure of Burkholderia glumae ToxA with bound S-adenosylhomocysteine (SAH) and 1,6-didemethyltoxoflavin==
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<StructureSection load='5je0' size='340' side='right' caption='[[5je0]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
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<StructureSection load='5je0' size='340' side='right'caption='[[5je0]], [[Resolution|resolution]] 1.55&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5je0]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JE0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JE0 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5je0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Burkholderia_glumae Burkholderia glumae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JE0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JE0 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=AZ8:PYRIMIDO[5,4-E][1,2,4]TRIAZINE-5,7(6H,8H)-DIONE'>AZ8</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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]] 1.552&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5je6|5je6]], [[5jdy|5jdy]], [[5jdz|5jdz]], [[5je1|5je1]], [[5je2|5je2]], [[5je3|5je3]], [[5je4|5je4]], [[5je5|5je5]]</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=AZ8:PYRIMIDO[5,4-E][1,2,4]TRIAZINE-5,7(6H,8H)-DIONE'>AZ8</scene>, <scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</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=5je0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5je0 OCA], [http://pdbe.org/5je0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5je0 RCSB], [http://www.ebi.ac.uk/pdbsum/5je0 PDBsum]</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=5je0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5je0 OCA], [https://pdbe.org/5je0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5je0 RCSB], [https://www.ebi.ac.uk/pdbsum/5je0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5je0 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/Q9LBJ0_BURGL Q9LBJ0_BURGL]
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Toxoflavin is a major virulence factor of the rice pathogen Burkholderia glumae. The tox operon of B. glumae contains five putative toxoflavin biosynthetic genes toxABCDE. ToxA is a predicted S-adenosylmethionine-dependent methyltransferase, and toxA knockouts of B. glumae are less virulent in plant infection models. In this study, we show that ToxA performs two consecutive methylations to convert the putative azapteridine intermediate, 1,6-didemethyltoxoflavin, to toxoflavin. In addition, we report a series of crystal structures of ToxA complexes that reveals the molecular basis of the dual methyltransferase activity. The results suggest sequential methylations with initial methylation at N6 of 1,6-didemethyltoxoflavin followed by methylation at N1. The two azapteridine orientations that position N6 or N1 for methylation are coplanar with a 140 degrees rotation between them. The structure of ToxA contains a class I methyltransferase fold having an N-terminal extension that either closes over the active site or is largely disordered. The ordered conformation places Tyr7 at a position of a structurally conserved tyrosine site of unknown function in various methyltransferases. Crystal structures of ToxA-Y7F consistently show a closed active site, whereas structures of ToxA-Y7A consistently show an open active site, suggesting that the hydroxyl group of Tyr7 plays a role in opening and closing the active site during the multistep reaction.
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Burkholderia glumae ToxA Is a Dual-Specificity Methyltransferase That Catalyzes the Last Two Steps of Toxoflavin Biosynthesis.,Fenwick MK, Philmus B, Begley TP, Ealick SE Biochemistry. 2016 May 3. PMID:27070241<ref>PMID:27070241</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 5je0" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Begley, T P]]
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[[Category: Burkholderia glumae]]
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[[Category: Ealick, S E]]
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[[Category: Large Structures]]
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[[Category: Fenwick, M K]]
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[[Category: Begley TP]]
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[[Category: Philmus, B]]
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[[Category: Ealick SE]]
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[[Category: Complex]]
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[[Category: Fenwick MK]]
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[[Category: N-methyltransferase]]
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[[Category: Philmus B]]
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[[Category: Substrate]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Burkholderia glumae ToxA with bound S-adenosylhomocysteine (SAH) and 1,6-didemethyltoxoflavin

PDB ID 5je0

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