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M206568200v1
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Papers In Press, published online ahead of print October 24, 2002
J. Biol. Chem, 10.1074/jbc.M206568200
Submitted on July 2, 2002
Revised on October 24, 2002
Accepted on October 24, 2002

Preliminary characterization and crystal structure of a thermostable cytochrome P450 from thermus thermophilus

Jason K. Yano, Francesca Blasco, Huiying Li, Rolf D. Schmid, Anke Henne, and Thomas L. Poulos

University of CAlif., Irvine, Irvine, CA 92697-3900

Corresponding Author: poulos{at}uci.edu

The second structure of a thermophile cytochrome P450, CYP175A1 from the thermophilic bacterium Thermus thermophilus HB27, has been solved to 1.8Å 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 thermal stable 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.


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