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5je3

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<StructureSection load='5je3' size='340' side='right'caption='[[5je3]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
<StructureSection load='5je3' size='340' side='right'caption='[[5je3]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5je3]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_33617 Atcc 33617]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JE3 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5je3]] 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=5JE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JE3 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=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]] 1.792&#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]], [[5je0|5je0]], [[5je1|5je1]], [[5je2|5je2]], [[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=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=337 ATCC 33617])</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=5je3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5je3 OCA], [https://pdbe.org/5je3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5je3 RCSB], [https://www.ebi.ac.uk/pdbsum/5je3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5je3 ProSAT]</span></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=5je3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5je3 OCA], [http://pdbe.org/5je3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5je3 RCSB], [http://www.ebi.ac.uk/pdbsum/5je3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5je3 ProSAT]</span></td></tr>
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</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 5je3" 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: Atcc 33617]]
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[[Category: Burkholderia glumae]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Begley, T P]]
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[[Category: Begley TP]]
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[[Category: Ealick, S E]]
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[[Category: Ealick SE]]
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[[Category: Fenwick, M K]]
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[[Category: Fenwick MK]]
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[[Category: Philmus, B]]
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[[Category: Philmus B]]
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[[Category: Mutant]]
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[[Category: N-methyltransferase]]
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[[Category: Product complex]]
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[[Category: Transferase]]
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Current revision

Crystal structure of Burkholderia glumae ToxA Y7A mutant with bound S-adenosylhomocysteine (SAH)

PDB ID 5je3

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