1n97

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Crystal Stucture of CYP175A1 from Thermus thermophillus strain HB27

Overview

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.

About this Structure

1N97 is a Single protein structure of sequence from Thermus thermophilus with SRT, HEM and EDO as ligands. Full crystallographic information is available from OCA.

Reference

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

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