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J. Biol. Chem., Vol. 275, Issue 40, 31086-31092, October 6, 2000
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From the 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 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/).
Crystal Structure of a Thermophilic Cytochrome P450 from the
Archaeon Sulfolobus solfataricus*
,,,¶
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
*
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.
Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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