The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre. |
| |
| Authors: | G?tz Hofhaus Jeung-Eun Lee Ivo Tews Beate Rosenberg Thomas Lisowsky |
| |
| Affiliation: | Institut für Biochemie und Biologisch-Medizinisches Forschungszentrum, Heinrich-Heine-Universit?t Düsseldorf, Germany. hofhaus@uni-duesseldorf.de |
| |
| Abstract: | Yeast Erv1p is a ubiquitous FAD-dependent sulfhydryl oxidase, located in the intermembrane space of mitochondria. The dimeric enzyme is essential for survival of the cell. Besides the redox-active CXXC motif close to the FAD, Erv1p harbours two additional cysteine pairs. Site-directed mutagenesis has identified all three cysteine pairs as essential for normal function. The C-terminal cysteine pair is of structural importance as it contributes to the correct arrangement of the FAD-binding fold. Variations in dimer formation and unique colour changes of mutant proteins argue in favour of an interaction between the N-terminal cysteine pair with the redox centre of the partner monomer. |
| |
| Keywords: | |
|
