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| | <StructureSection load='1f4t' size='340' side='right'caption='[[1f4t]], [[Resolution|resolution]] 1.93Å' scene=''> | | <StructureSection load='1f4t' size='340' side='right'caption='[[1f4t]], [[Resolution|resolution]] 1.93Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1f4t]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4T OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1F4T FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1f4t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F4T 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=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </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=PIM:4-PHENYL-1H-IMIDAZOLE'>PIM</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1f4u|1f4u]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1f4u|1f4u]]</div></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=1f4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4t OCA], [http://pdbe.org/1f4t PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1f4t RCSB], [http://www.ebi.ac.uk/pdbsum/1f4t PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4t 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=1f4t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f4t OCA], [https://pdbe.org/1f4t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f4t RCSB], [https://www.ebi.ac.uk/pdbsum/1f4t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f4t ProSAT]</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]] |
| 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
The structure of the first P450 identified in Archaea, CYP119 from Sulfolobus solfataricus, has been solved in two different crystal forms that differ by the ligand (imidazole or 4-phenylimidazole) coordinated to the heme iron. A comparison of the two structures reveals an unprecedented rearrangement of the active site to adapt to the different size and shape of ligands bound to the heme iron. These changes involve unraveling of the F helix C-terminal segment to extend a loop structure connecting the F and G helices, allowing the longer loop to dip down into the active site and interact with the smaller imidazole ligand. A comparison of CYP119 with P450cam and P450eryF indicates an extensive clustering of aromatic residues may provide the structural basis for the enhanced thermal stability of CYP119. An additional feature of the 4-phenylimidazole-bound structure is a zinc ion tetrahedrally bound by symmetry-related His and Glu residues.
Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus.,Yano JK, Koo LS, Schuller DJ, Li H, Ortiz de Montellano PR, Poulos TL J Biol Chem. 2000 Oct 6;275(40):31086-92. PMID:10859321[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
- ↑ Yano JK, Koo LS, Schuller DJ, Li H, Ortiz de Montellano PR, Poulos TL. Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus. J Biol Chem. 2000 Oct 6;275(40):31086-92. PMID:10859321 doi:10.1074/jbc.M004281200
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