Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus.,Yano JK, Blasco F, Li H, Schmid RD, Henne A, Poulos TL J Biol Chem. 2003 Jan 3;278(1):608-16. Epub 2002 Oct 24. PMID:12401810[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Yano JK, Blasco F, Li H, Schmid RD, Henne A, Poulos TL. Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus. J Biol Chem. 2003 Jan 3;278(1):608-16. Epub 2002 Oct 24. PMID:12401810 doi:10.1074/jbc.M206568200
