The cupredoxin fold is found in the soluble CuA and CyoA domains of two terminal oxidases

FEBS Letters

Källebring, Bruno²  Wittung, Pernilla¹  Malmström, Bo G.² 

[1] Department of Physical Chemistry, Chalmers University of Technology, S-412 96 Göteborg, Sweden;Department of Biochemistry and Biophysics, Göteborg University, Medicinaregatan 9C, S-413 90 Göteborg, Sweden

关键词: Cytochrome oxidase;    Quinol oxidase;    Azurin;    Plastocyanin;    Circular dichroism;    Protein secondary structure;   

DOI  :  10.1016/0014-5793(94)00694-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The CD spectra of the Cu_A domain from subunit II of Paracoccus cytochrome c oxidase and the CyoA domain of subunit II from E. coli quinol oxidase have been recorded in the wavelength region 260-185 nm. A computer program based on a set of CD spectra of proteins with known structures, and employing the stastistical method of variable selection, has been used to estimate the distribution of five forms of secondary structure. The analysis was improved by including the CD spectra of azurin and plastocyanin in the basis set. For the Cu_A domain, an estimate from the primary structure was also made. The results show that the soluble domains have the cupredoxin fold, with very little helical structure and a predominance of β-strands. The CyoA domain is very similar to azurin, but the β-structure in the Cu_A protein resembles that in plastocyanin.

【 授权许可】

Unknown