1f4t: Difference between revisions

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New page: left|200px<br /><applet load="1f4t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f4t, resolution 1.93Å" /> '''THERMOPHILIC P450: C...
 
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[[Image:1f4t.jpg|left|200px]]<br /><applet load="1f4t" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f4t, resolution 1.93&Aring;" />
'''THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND'''<br />


==Overview==
==THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND==
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.
<StructureSection load='1f4t' size='340' side='right'caption='[[1f4t]], [[Resolution|resolution]] 1.93&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f4t]] 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=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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.93&#8491;</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='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>
== Function ==
[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]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f4/1f4t_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1f4t ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== 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.


==About this Structure==
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<ref>PMID:10859321</ref>
1F4T is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus] with ZN, SO4, HEM and PIM as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F4T OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10859321 10859321]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1f4t" style="background-color:#fffaf0;"></div>
[[Category: Sulfolobus solfataricus]]
== References ==
[[Category: Koo, L.S.]]
<references/>
[[Category: Li, H.]]
__TOC__
[[Category: Montellano, P.R.Ortiz.de.]]
</StructureSection>
[[Category: Poulos, T.L.]]
[[Category: Large Structures]]
[[Category: Schuller, D.J.]]
[[Category: Saccharolobus solfataricus]]
[[Category: Yano, J.K.]]
[[Category: Koo LS]]
[[Category: HEM]]
[[Category: Li H]]
[[Category: PIM]]
[[Category: Ortiz de Montellano PR]]
[[Category: SO4]]
[[Category: Poulos TL]]
[[Category: ZN]]
[[Category: Schuller DJ]]
[[Category: p450 fold]]
[[Category: Yano JK]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:37:04 2007''

Latest revision as of 05:53, 13 August 2026

THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND

1f4t, resolution 1.93Å

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