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| | <StructureSection load='4at2' size='340' side='right'caption='[[4at2]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='4at2' size='340' side='right'caption='[[4at2]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4at2]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Rhojr Rhojr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AT2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4AT2 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4at2]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhodococcus_jostii_RHA1 Rhodococcus jostii RHA1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AT2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AT2 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</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">X-ray diffraction, [[Resolution|Resolution]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4at0|4at0]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ASD:4-ANDROSTENE-3-17-DIONE'>ASD</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/3-oxo-5-alpha-steroid_4-dehydrogenase_(acceptor) 3-oxo-5-alpha-steroid 4-dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.3.99.5 1.3.99.5] </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=4at2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4at2 OCA], [https://pdbe.org/4at2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4at2 RCSB], [https://www.ebi.ac.uk/pdbsum/4at2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4at2 ProSAT]</span></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=4at2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4at2 OCA], [http://pdbe.org/4at2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4at2 RCSB], [http://www.ebi.ac.uk/pdbsum/4at2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4at2 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q0S4Q9_RHOJR Q0S4Q9_RHOJR] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Rhojr]] | + | [[Category: Large Structures]] |
| - | [[Category: Dijkhuizen, L]] | + | [[Category: Rhodococcus jostii RHA1]] |
| - | [[Category: Dijkstra, B W]] | + | [[Category: Dijkhuizen L]] |
| - | [[Category: Geize, R van der]] | + | [[Category: Dijkstra BW]] |
| - | [[Category: Knol, J]] | + | [[Category: Knol J]] |
| - | [[Category: Oosterwijk, N van]] | + | [[Category: Van Oosterwijk N]] |
| - | [[Category: Oxidoreductase]] | + | [[Category: Van der Geize R]] |
| - | [[Category: Steroid catabolism]]
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| Structural highlights
Function
Q0S4Q9_RHOJR
Publication Abstract from PubMed
3-Ketosteroid Delta4-(5alpha)-dehydrogenases (Delta4-(5alpha)-KSTDs) are enzymes that introduce a double bond between the C4 and C5 atoms of 3-keto-(5alpha)-steroids. Here we show that the ro05698 gene from Rhodococcus jostii RHA1 codes for a flavoprotein with Delta4-(5alpha)-KSTD activity. The 1.6 A resolution crystal structure of the enzyme revealed three conserved residues (Tyr-319, Tyr-466, and Ser-468) in a pocket near the isoalloxazine ring system of the FAD co-factor. Site-directed mutagenesis of these residues confirmed that they are absolutely essential for catalytic activity. A crystal structure with bound product 4-androstene-3,17-dione showed that Ser-468 is in a position in which it can serve as the base abstracting the 4beta-proton from the C4 atom of the substrate. Ser-468 is assisted by Tyr-319, which possibly is involved in shuttling the proton to the solvent. Tyr-466 is at hydrogen bonding distance to the C3 oxygen atom of the substrate and can stabilize the keto-enol intermediate occurring during the reaction. Finally, the FAD N5 atom is in a position to be able to abstract the 5alpha-hydrogen of the substrate as a hydride ion. These features fully explain the reaction catalyzed by Delta4-(5alpha)-KSTDs.
Structure and Catalytic Mechanism of 3-Ketosteroid-{Delta}4-(5alpha)-dehydrogenase from Rhodococcus jostii RHA1 Genome.,van Oosterwijk N, Knol J, Dijkhuizen L, van der Geize R, Dijkstra BW J Biol Chem. 2012 Sep 7;287(37):30975-83. Epub 2012 Jul 24. PMID:22833669[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ van Oosterwijk N, Knol J, Dijkhuizen L, van der Geize R, Dijkstra BW. Structure and Catalytic Mechanism of 3-Ketosteroid-{Delta}4-(5alpha)-dehydrogenase from Rhodococcus jostii RHA1 Genome. J Biol Chem. 2012 Sep 7;287(37):30975-83. Epub 2012 Jul 24. PMID:22833669 doi:http://dx.doi.org/10.1074/jbc.M112.374306
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