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1io9

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Revision as of 11:02, 4 August 2021

THERMOPHILIC CYTOCHROME P450 (CYP119) FROM SULFOLOBUS SOLFATARICUS: HIGH RESOLUTION STRUCTURAL ORIGIN OF ITS THERMOSTABILITY AND FUNCTIONAL PROPERTIES

Structural highlights

1io9 is a 2 chain structure with sequence from Atcc 35091. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1io7, 1io8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT, TOPSAN

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1io9"

@@ Line 3: / Line 3: @@
 <StructureSection load='1io9' size='340' side='right'caption='[[1io9]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1io9]] 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=1IO9 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IO9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1io9]] 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=1IO9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IO9 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='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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1io7|1io7]], [[1io8|1io8]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1io7|1io7]], [[1io8|1io8]]</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=1io9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io9 OCA], [http://pdbe.org/1io9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1io9 RCSB], [http://www.ebi.ac.uk/pdbsum/1io9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1io9 ProSAT], [http://www.topsan.org/Proteins/RSGI/1io9 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=1io9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1io9 OCA], [https://pdbe.org/1io9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1io9 RCSB], [https://www.ebi.ac.uk/pdbsum/1io9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1io9 ProSAT], [https://www.topsan.org/Proteins/RSGI/1io9 TOPSAN]</span></td></tr>
 </table>
 == 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 ==
 [[Image:Consurf_key_small.gif|200px|right]]

1io9

From Proteopedia

Revision as of 11:02, 4 August 2021

THERMOPHILIC CYTOCHROME P450 (CYP119) FROM SULFOLOBUS SOLFATARICUS: HIGH RESOLUTION STRUCTURAL ORIGIN OF ITS THERMOSTABILITY AND FUNCTIONAL PROPERTIES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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