|
|
| Line 3: |
Line 3: |
| <StructureSection load='6a7j' size='340' side='right'caption='[[6a7j]], [[Resolution|resolution]] 2.71Å' scene=''> | | <StructureSection load='6a7j' size='340' side='right'caption='[[6a7j]], [[Resolution|resolution]] 2.71Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
| <table><tr><td colspan='2'>[[6a7j]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"actinomyces_violaceus-ruber"_(sic)_waksman_and_curtis_1916 "actinomyces violaceus-ruber" (sic) waksman and curtis 1916]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A7J OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6A7J FirstGlance]. <br> | | <table><tr><td colspan='2'>[[6a7j]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptomyces_violaceoruber Streptomyces violaceoruber]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A7J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A7J FirstGlance]. <br> |
| </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TES:TESTOSTERONE'>TES</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]] 2.71Å</td></tr> |
| <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">B1H20_20375 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1935 "Actinomyces violaceus-ruber" (sic) Waksman and Curtis 1916])</td></tr> | | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=TES:TESTOSTERONE'>TES</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=6a7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7j OCA], [http://pdbe.org/6a7j PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a7j RCSB], [http://www.ebi.ac.uk/pdbsum/6a7j PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7j 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=6a7j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a7j OCA], [https://pdbe.org/6a7j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a7j RCSB], [https://www.ebi.ac.uk/pdbsum/6a7j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a7j ProSAT]</span></td></tr> |
| </table> | | </table> |
| <div style="background-color:#fffaf0;">
| | == Function == |
| == Publication Abstract from PubMed == | | [https://www.uniprot.org/uniprot/A0A1V0UEC8_STRVN A0A1V0UEC8_STRVN] |
| Bacterial cytochrome P450 (CYP) enzymes are involved in the hydroxylation of various endogenous substrates while using a heme molecule as a cofactor. CYPs have gained biotechnological interest as useful biocatalysts capable of altering chemical structures by adding a hydroxyl group in a regiospecific manner. Here, we identified, purified, and characterized two CYP154C4 proteins from Streptomyces sp. W2061 (StCYP154C4-1) and Streptomyces sp. ATCC 11861 (StCYP154C4-2). Activity assays showed that both StCYP154C4-1 and StCYP154C4-2 can produce 2'-hydroxylated testosterone, which differs from the activity of a previously described NfCYP154C5 from Nocardia farcinica in terms of its 16alpha-hydroxylation of testosterone. To better understand the molecular basis of the regioselectivity of these two CYP154C4 proteins, crystal structures of the ligand-unbound form of StCYP154C4-1 and the testosterone-bound form of StCYP154C4-2 were determined. Comparison with the previously determined NfCYP154C5 structure revealed differences in the substrate-binding residues, suggesting a likely explanation for the different patterns of testosterone hydroxylation, despite the high sequence similarities between the enzymes (54% identity). These findings provide valuable insights that will enable protein engineering for the development of artificial steroid-related CYPs exhibiting different regiospecificity.
| |
|
| |
|
| Characterization of two steroid hydroxylases from different Streptomyces spp. and their ligand-bound and -unbound crystal structures.,Dangi B, Lee CW, Kim KH, Park SH, Yu EJ, Jeong CS, Park H, Lee JH, Oh TJ FEBS J. 2018 Dec 15. doi: 10.1111/febs.14729. PMID:30552795<ref>PMID:30552795</ref>
| | ==See Also== |
| | | *[[Cytochrome P450 3D structures|Cytochrome P450 3D structures]] |
| From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| |
| </div>
| |
| <div class="pdbe-citations 6a7j" style="background-color:#fffaf0;"></div>
| |
| == References == | |
| <references/>
| |
| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Lee, C W]] | | [[Category: Streptomyces violaceoruber]] |
| [[Category: Lee, J H]] | | [[Category: Lee CW]] |
| [[Category: Cytochrome p450]] | | [[Category: Lee JH]] |
| [[Category: Oxidoreductase]]
| |
| [[Category: Steroid hydroxylase]]
| |
| [[Category: Streptomyce]]
| |
