1N97

Crystal Structure of CYP175A1 from Thermus thermophillus strain HB27

Summary for 1N97

• Entry DOI: 10.2210/pdb1n97/pdb
• Descriptor: CYP175A1, S,R MESO-TARTARIC ACID, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total)
• Functional Keywords: p450, electron transport
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 91294.94

Authors

Yano, J.K.,Blasco, F.,Li, H.,Schmid, R.D.,Henne, A.,Poulos, T.L. (deposition date: 2002-11-22, release date: 2003-02-25, Last modification date: 2023-08-16)

Primary citation

Yano, J.K.,Blasco, F.,Li, H.,Schmid, R.D.,Henne, A.,Poulos, T.L.
Preliminary Characterization and Crystal Structure of a Thermostable Cytochrome P450 from Thermus thermophilus
J.Biol.Chem., 278:608-616, 2003

PubMed Abstract: 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.

PubMed: 12401810
DOI: 10.1074/jbc.M206568200

Experimental method

X-RAY DIFFRACTION (1.8 Å)