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| | <StructureSection load='1io7' size='340' side='right'caption='[[1io7]], [[Resolution|resolution]] 1.50Å' scene=''> | | <StructureSection load='1io7' size='340' side='right'caption='[[1io7]], [[Resolution|resolution]] 1.50Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1io7]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IO7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1io7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharolobus_solfataricus Saccharolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IO7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO7 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></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]] 1.5Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1io8|1io8]], [[1io9|1io9]]</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></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=1io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io7 OCA], [http://pdbe.org/1io7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1io7 RCSB], [http://www.ebi.ac.uk/pdbsum/1io7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1io7 ProSAT], [http://www.topsan.org/Proteins/RSGI/1io7 TOPSAN]</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=1io7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io7 OCA], [https://pdbe.org/1io7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io7 RCSB], [https://www.ebi.ac.uk/pdbsum/1io7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io7 ProSAT], [https://www.topsan.org/Proteins/RSGI/1io7 TOPSAN]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CP119_SULAC CP119_SULAC]] The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid.<ref>PMID:10799487</ref> <ref>PMID:12010041</ref> <ref>PMID:18157853</ref> | + | [https://www.uniprot.org/uniprot/CP119_SULAC CP119_SULAC] The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid.<ref>PMID:10799487</ref> <ref>PMID:12010041</ref> <ref>PMID:18157853</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Adachi, S]] | + | [[Category: Saccharolobus solfataricus]] |
| - | [[Category: Park, S Y]] | + | [[Category: Adachi S]] |
| - | [[Category: Structural genomic]] | + | [[Category: Park S-Y]] |
| - | [[Category: Shiro, Y]] | + | [[Category: Shiro Y]] |
| - | [[Category: Sligar, S G]] | + | [[Category: Sligar SG]] |
| - | [[Category: Yamane, K]] | + | [[Category: Yamane K]] |
| - | [[Category: Cytochromo p450]]
| + | |
| - | [[Category: Oxidoreductase]]
| + | |
| - | [[Category: Rsgi]]
| + | |
| - | [[Category: Thermophilic]]
| + | |
| Structural highlights
Function
CP119_SULAC The endogenous substrate is not known. In vitro, catalyzes the H(2)O(2)-dependent epoxidation of styrene, cis-beta-methylstyrene, and cis-stilbene with retention of stereochemistry. Is able to use cumene hydroperoxide (CHP) or tert-butyl hydroperoxide (TBHP) instead of H(2)O(2) as the electron acceptor. Can also hydroxylate fatty acids such as lauric acid.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Crystal structures of a thermostable cytochrome P450 (CYP119) and a site-directed mutant, (Phe24Leu), from the acidothermophilic archaea Sulfolobus solfataricus were determined at 1.5-2.0 A resolution. We identify important crystallographic waters in the ferric heme pocket, observe protein conformational changes upon inhibitor binding, and detect a unique distribution of surface charge not found in other P450s. An analysis of factors contributing to thermostability of CYP119 of these high resolution structures shows an apparent increase in clustering of aromatic residues and optimum stacking. The contribution of aromatic stacking was investigated further with the mutant crystal structure and differential scanning calorimetry.
Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties.,Park SY, Yamane K, Adachi S, Shiro Y, Weiss KE, Maves SA, Sligar SG J Inorg Biochem. 2002 Sep 20;91(4):491-501. PMID:12237217[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Koo LS, Tschirret-Guth RA, Straub WE, Moenne-Loccoz P, Loehr TM, Ortiz de Montellano PR. The active site of the thermophilic CYP119 from Sulfolobus solfataricus. J Biol Chem. 2000 May 12;275(19):14112-23. PMID:10799487
- ↑ Koo LS, Immoos CE, Cohen MS, Farmer PJ, Ortiz de Montellano PR. Enhanced electron transfer and lauric acid hydroxylation by site-directed mutagenesis of CYP119. J Am Chem Soc. 2002 May 22;124(20):5684-91. PMID:12010041
- ↑ Rabe KS, Kiko K, Niemeyer CM. Characterization of the peroxidase activity of CYP119, a thermostable P450 from Sulfolobus acidocaldarius. Chembiochem. 2008 Feb 15;9(3):420-5. PMID:18157853 doi:http://dx.doi.org/10.1002/cbic.200700450
- ↑ Park SY, Yamane K, Adachi S, Shiro Y, Weiss KE, Maves SA, Sligar SG. Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties. J Inorg Biochem. 2002 Sep 20;91(4):491-501. PMID:12237217
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