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| | ==Joint X-ray Neutron Structure of Cholesterol Oxidase== | | ==Joint X-ray Neutron Structure of Cholesterol Oxidase== |
| - | <StructureSection load='5kwf' size='340' side='right' caption='[[5kwf]], [[Resolution|resolution]] 1.50Å' scene=''> | + | <StructureSection load='5kwf' size='340' side='right'caption='[[5kwf]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5kwf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strs0 Strs0]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KWF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5KWF FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5kwf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_sp._SA-COO Streptomyces sp. SA-COO]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5KWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5KWF FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Hybrid , Neutron Diffraction , X-ray diffraction, [[Resolution|Resolution]] 1.499Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">choA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=74576 STRS0])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DOD:DEUTERATED+WATER'>DOD</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5kwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kwf OCA], [http://pdbe.org/5kwf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5kwf RCSB], [http://www.ebi.ac.uk/pdbsum/5kwf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5kwf 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=5kwf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5kwf OCA], [https://pdbe.org/5kwf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5kwf RCSB], [https://www.ebi.ac.uk/pdbsum/5kwf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5kwf ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CHOD_STRS0 CHOD_STRS0]] Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product. | + | [https://www.uniprot.org/uniprot/CHOD_STRS0 CHOD_STRS0] Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 5kwf" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 5kwf" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Cholesterol oxidase|Cholesterol oxidase]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Strs0]] | + | [[Category: Large Structures]] |
| - | [[Category: Blakeley, M]] | + | [[Category: Streptomyces sp. SA-COO]] |
| - | [[Category: Golden, E]] | + | [[Category: Blakeley M]] |
| - | [[Category: Meilleur, F]] | + | [[Category: Golden E]] |
| - | [[Category: Vrielink, A]] | + | [[Category: Meilleur F]] |
| - | [[Category: Isomerase]]
| + | [[Category: Vrielink A]] |
| - | [[Category: Oxidoreductase]]
| + | |
| Structural highlights
Function
CHOD_STRS0 Bifunctional enzyme that catalyzes the oxidation of the 3-beta-hydroxy group of cholesterol and the isomerization of the double bond of the resulting product.
Publication Abstract from PubMed
The protein microenvironment surrounding the flavin cofactor in flavoenzymes is key to the efficiency and diversity of reactions catalysed by this class of enzymes. X-ray diffraction structures of oxidoreductase flavoenzymes have revealed recurrent features which facilitate catalysis, such as a hydrogen bond between a main chain nitrogen atom and the flavin redox center (N5). A neutron diffraction study of cholesterol oxidase has revealed an unusual elongated main chain nitrogen to hydrogen bond distance positioning the hydrogen atom towards the flavin N5 reactive center. Investigation of the structural features which could cause such an unusual occurrence revealed a positively charged lysine side chain, conserved in other flavin mediated oxidoreductases, in a second shell away from the FAD cofactor acting to polarize the peptide bond through interaction with the carbonyl oxygen atom. Double-hybrid density functional theory calculations confirm that this electrostatic arrangement affects the N-H bond length in the region of the flavin reactive center. We propose a novel second-order partial-charge interaction network which enables the correct orientation of the hydride receiving orbital of N5. The implications of these observations for flavin mediated redox chemistry are discussed.
An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase.,Golden E, Yu LJ, Meilleur F, Blakeley MP, Duff AP, Karton A, Vrielink A Sci Rep. 2017 Jan 18;7:40517. doi: 10.1038/srep40517. PMID:28098177[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Golden E, Yu LJ, Meilleur F, Blakeley MP, Duff AP, Karton A, Vrielink A. An extended N-H bond, driven by a conserved second-order interaction, orients the flavin N5 orbital in cholesterol oxidase. Sci Rep. 2017 Jan 18;7:40517. doi: 10.1038/srep40517. PMID:28098177 doi:http://dx.doi.org/10.1038/srep40517
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