Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus.
The second structure of a thermophile cytochrome P450, CYP175A1 from the thermophilic bacterium Thermus thermophilus HB27, has been solved to 1.8-A 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.
Yano
Jason K
JK
Department of Molecular Biology and Biochemistry, University of California, Irvine, California 92697-3900, USA.
Blasco
Francesca
F
Li
Huiying
H
Schmid
Rolf D
RD
Henne
Anke
A
Poulos
Thomas L
TL
D000818:Animals; D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D003460:Crystallization; D018360:Crystallography, X-Ray; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D004795:Enzyme Stability; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D013696:Temperature; D016963:Thermus thermophilus / Q000201:enzymology* / Q000235:genetics
D001426:Bacterial Proteins; D003577:Cytochrome P-450 Enzyme System