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Originally published In Press as doi:10.1074/jbc.M004281200 on June 19, 2000

J. Biol. Chem., Vol. 275, Issue 40, 31086-31092, October 6, 2000
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Crystal Structure of a Thermophilic Cytochrome P450 from the Archaeon Sulfolobus solfataricus*

Jason K. YanoDagger , Laura S. Koo§, David J. SchullerDagger , Huiying LiDagger , Paul R. Ortiz de Montellano§, and Thomas L. PoulosDagger

From the Dagger  Department of Molecular Biology and Biochemistry and Program in Macromolecular Structure, University of California, Irvine, California 92697-3900 and the § Department of Pharmaceutical Chemistry, School of Pharmacy, University of California, San Francisco, California 94143-0446

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.

* This work was supported by National Institutes of Health Grants GM32688 (to T. L. P.) and GM25515 (to P. O. M.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The atomic coordinates and the structure factors (code 1F4U, 1F4T) have been deposited in the Protein Data Bank, Research Collaboratory for Structural Bioinformatics, Rutgers University, New Brunswick, NJ (http://www.rcsb.org/).

To whom correspondence should be addressed. Tel.: 949-824-7020; Fax: 949-824-3280; E-mail: poulos@uci.edu.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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