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"  
[[Image:1f4t.jpg|left|200px]]<br /><applet load="1f4t" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1f4t, resolution 1.93&Aring;" />
caption="1f4t, resolution 1.93&Aring;" />
'''THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND'''<br />
'''THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND'''<br />


==Overview==
==Overview==
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.
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==
==About this Structure==
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].  
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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene>, <scene name='pdbligand=HEM:'>HEM</scene> and <scene name='pdbligand=PIM:'>PIM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F4T OCA].  


==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Sulfolobus solfataricus]]
[[Category: Sulfolobus solfataricus]]
[[Category: Koo, L.S.]]
[[Category: Koo, L S.]]
[[Category: Li, H.]]
[[Category: Li, H.]]
[[Category: Montellano, P.R.Ortiz.de.]]
[[Category: Montellano, P R.Ortiz de.]]
[[Category: Poulos, T.L.]]
[[Category: Poulos, T L.]]
[[Category: Schuller, D.J.]]
[[Category: Schuller, D J.]]
[[Category: Yano, J.K.]]
[[Category: Yano, J K.]]
[[Category: HEM]]
[[Category: HEM]]
[[Category: PIM]]
[[Category: PIM]]
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[[Category: p450 fold]]
[[Category: p450 fold]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 14:37:04 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:34:54 2008''

Revision as of 13:35, 21 February 2008

File:1f4t.jpg


1f4t, resolution 1.93Å

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

OverviewOverview

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 StructureAbout this Structure

1F4T is a Single protein structure of sequence from Sulfolobus solfataricus with , , and as ligands. Full crystallographic information is available from OCA.

ReferenceReference

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

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