7oud

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Current revision (07:51, 1 May 2024) (edit) (undo)
 
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<StructureSection load='7oud' size='340' side='right'caption='[[7oud]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
<StructureSection load='7oud' size='340' side='right'caption='[[7oud]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[7oud]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OUD FirstGlance]. <br>
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<table><tr><td colspan='2'>[[7oud]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._JP95 Streptomyces sp. JP95]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OUD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OUD FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1J0:Collinone'>1J0</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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]] 2.3&#8491;</td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7ouc|7ouc]]</div></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=1J0:Collinone'>1J0</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</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=7oud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oud OCA], [https://pdbe.org/7oud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oud RCSB], [https://www.ebi.ac.uk/pdbsum/7oud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oud 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=7oud FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oud OCA], [https://pdbe.org/7oud PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oud RCSB], [https://www.ebi.ac.uk/pdbsum/7oud PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oud 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/Q8KSX7_9ACTN Q8KSX7_9ACTN]
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The medically important bacterial aromatic polyketide natural products typically feature a planar, polycyclic core structure. An exception is found for the rubromycins, whose backbones are disrupted by a bisbenzannulated [5,6]-spiroketal pharmacophore that was recently shown to be assembled by flavin-dependent enzymes. In particular, a flavoprotein monooxygenase proved critical for the drastic oxidative rearrangement of a pentangular precursor and the installment of an intermediate [6,6]-spiroketal moiety. Here we provide structural and mechanistic insights into the control of catalysis by this spiroketal synthase, which fulfills several important functions as reductase, monooxygenase, and presumably oxidase. The enzyme hereby tightly controls the redox state of the substrate to counteract shunt product formation, while also steering the cleavage of three carbon-carbon bonds. Our work illustrates an exceptional strategy for the biosynthesis of stable chroman spiroketals.
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Catalytic Control of Spiroketal Formation in Rubromycin Polyketide Biosynthesis.,Teufel R, Toplak M, Saleem-Batcha R, Piel J Angew Chem Int Ed Engl. 2021 Oct 15. doi: 10.1002/anie.202109384. PMID:34652045<ref>PMID:34652045</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 7oud" 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]]
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[[Category: Saleem-Batcha, R]]
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[[Category: Streptomyces sp. JP95]]
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[[Category: Teufel, R]]
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[[Category: Saleem-Batcha R]]
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[[Category: Toplak, M]]
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[[Category: Teufel R]]
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[[Category: Flavoprotein]]
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[[Category: Toplak M]]
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[[Category: Griseorhodin a biosynthesis]]
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[[Category: Monooxygenase]]
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[[Category: Rubromycin biosynthesis]]
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Current revision

Crystal structure of a ternary complex of the flavoprotein monooxygenase GrhO5 with FAD and collinone

PDB ID 7oud

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