1f4t: Difference between revisions

Revision as of 02:41, 1 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1f4t.png

Template:STRUCTURE 1f4t

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

Template:ABSTRACT PUBMED 10859321

About this StructureAbout this Structure

1F4T is a Single protein structure of sequence from Sulfolobus solfataricus. 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

Page seeded by OCA on Tue Jul 1 02:41:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND'''
+===THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS WITH 4-PHENYLIMIDAZOLE BOUND===
-==Overview==
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-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 line below this paragraph, {{ABSTRACT_PUBMED_10859321}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_10859321}}
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 [[Category: Yano, J K.]]
 [[Category: P450 fold]]
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