6wn3: Difference between revisions

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<StructureSection load='6wn3' size='340' side='right'caption='[[6wn3]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
<StructureSection load='6wn3' size='340' side='right'caption='[[6wn3]], [[Resolution|resolution]] 1.86&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6wn3]] 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=6WN3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6WN3 FirstGlance]. <br>
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WN3 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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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]] 1.86&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">sxtT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=467598 Lyngbya wollei])</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>, <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'>[http://proteopedia.org/fgij/fg.htm?mol=6wn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wn3 OCA], [http://pdbe.org/6wn3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6wn3 RCSB], [http://www.ebi.ac.uk/pdbsum/6wn3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6wn3 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=6wn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6wn3 OCA], [https://pdbe.org/6wn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6wn3 RCSB], [https://www.ebi.ac.uk/pdbsum/6wn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6wn3 ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
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>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6wn3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__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]]
[[Category: Metalloprotein]]
[[Category: Natural product]]
[[Category: Rieske oxygenase]]
[[Category: Saxitoxin]]
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