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J. Biol. Chem., Vol. 278, Issue 1, 608-616, January 3, 2003
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From the The second structure of a thermophile cytochrome
P450, CYP175A1 from the thermophilic bacterium Thermus
thermophilus HB27, has been solved to 1.8-Å resolution. The
overall P450 structure remains conserved despite the low sequence
identity between the various P450s. The CYP175A1 structure lacks the
large aromatic network found in the only other thermostable P450,
CYP119, thought to contribute to thermal stability. The primary
difference between CYP175A1 and its mesophile counterparts is the
investment of charged residues into salt-link networks at the expense
of single charge-charge interactions. Additional factors involved in
the thermal stability increase are a decrease in the overall size,
especially shortening of loops and connecting regions, and a
decrease in the number of labile residues such as Asn, Gln, and Cys.
Preliminary Characterization and Crystal Structure of a
Thermostable Cytochrome P450 from Thermus thermophilus*
,,
Department of Molecular Biology and
Biochemistry, the Department of Physiology and Biophysics, and the
Program in Macromolecular Structure, University of California, Irvine,
California 92697-3900, the § Institut fur Technische
Biochemie, Universität Stuttgart, Allmandring 31, D-70569
Stuttgart, Germany, and the ¶ Institute of Microbiology and
Genetics, University of Göttingen, Grisebachstrasse 8, 37077 Göttingen, Germany
*
This work was supported by National Institutes of Health
Grant GM32688 (to T. L. P.) and by a grant from BASF AG,
Ludwigshafen, Germany (to R. D. S.).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.
To whom correspondence should be addressed. Tel.:
949-824-7020; Fax: 949-824-3280; E-mail: poulos@uci.edu.
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