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Papers In Press, published online ahead of print June 19, 2000
J. Biol. Chem, 10.1074/jbc.M004281200
Submitted on May 18, 2000
Revised on June 15, 2000
Accepted on June 15, 2000

Crystal Structure of a Thermophilic Cytochrome P450 from the Archaeon Sulfolobus solfataricus

Jason K. Yano, Laura S. Koo, David J. Schuller, Huiying Li, Paul R. Ortiz de Montellano, and Thomas L. Poulos

University of California, Irvine, Irvine, CA 92697-3900

Corresponding Author: poulos{at}uci.edu

The structure of the first P450 identified in archaea, CYP119 from Sulfolobus solfataricus, has been solved in 2 different crystal forms. The first form has imidazole and the second has 4-phenylimidazole coordinated to the heme iron. A comparison of the 2 structures reveals an unprecedented rearrangement of the active site in order 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 in order 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 be 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.


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