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| <StructureSection load='6wnc' size='340' side='right'caption='[[6wnc]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='6wnc' size='340' side='right'caption='[[6wnc]], [[Resolution|resolution]] 2.20Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6wnc]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Lyngbya_wollei Lyngbya wollei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WNC OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WNC FirstGlance]. <br> | | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WNC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WNC FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6wn3|6wn3]]</td></tr>
| | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene>, <scene name='pdbligand=FES:FE2/S2+(INORGANIC)+CLUSTER'>FES</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sxtDIOX ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=467598 Lyngbya wollei])</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=6wnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wnc OCA], [https://pdbe.org/6wnc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wnc RCSB], [https://www.ebi.ac.uk/pdbsum/6wnc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wnc ProSAT]</span></td></tr> |
| <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6wnc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wnc OCA], [http://pdbe.org/6wnc PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wnc RCSB], [http://www.ebi.ac.uk/pdbsum/6wnc PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wnc ProSAT]</span></td></tr> | |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
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| == Publication Abstract from PubMed ==
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| Biocatalysts that perform C-H hydroxylation exhibit exceptional substrate specificity and site-selectivity, often through the use of high valent oxidants to activate these inert bonds. Rieske oxygenases are examples of enzymes with the ability to perform precise mono- or dioxygenation reactions on a variety of substrates. Understanding the structural features of Rieske oxygenases responsible for control over selectivity is essential to enable the development of this class of enzymes for biocatalytic applications. Decades of research has illuminated the critical features common to Rieske oxygenases, however, structural information for enzymes that functionalize diverse scaffolds is limited. Here, we report the structures of two Rieske monooxygenases involved in the biosynthesis of paralytic shellfish toxins (PSTs), SxtT and GxtA, adding to the short list of structurally characterized Rieske oxygenases. Based on these structures, substrate-bound structures, and mutagenesis experiments, we implicate specific residues in substrate positioning and the divergent reaction selectivity observed in these two enzymes.
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| Structural basis for divergent C-H hydroxylation selectivity in two Rieske oxygenases.,Lukowski AL, Liu J, Bridwell-Rabb J, Narayan ARH Nat Commun. 2020 Jun 12;11(1):2991. doi: 10.1038/s41467-020-16729-0. PMID:32532989<ref>PMID:32532989</ref>
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| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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| </div>
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| <div class="pdbe-citations 6wnc" style="background-color:#fffaf0;"></div>
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| == References ==
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| <references/>
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lyngbya wollei]]
| | [[Category: Bridwell-Rabb J]] |
| [[Category: Bridwell-Rabb, J]] | | [[Category: Liu J]] |
| [[Category: Liu, J]] | |
| [[Category: Biosynthetic protein]]
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| [[Category: Metalloprotein]]
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| [[Category: Natural product]]
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| [[Category: Rieske oxygenase]]
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| [[Category: Saxitoxin]]
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