Article
Binding of sulfurated molybdenum cofactor to the C-terminal domain of ABA3 from Arabidopsis thaliana provides insight into the mechanism of molybdenum cofactor sulfuration.
The Journal of biological chemistry - 11 Apr 2008
Wollers Silke, Heidenreich Torsten, Zarepour Maryam, Zachmann Dieter, Kraft Claudia, Zhao Yunde, Mendel Ralf R, Bittner Florian
Abstract excerpt
The molybdenum cofactor sulfurase ABA3 from Arabidopsis thaliana is needed for post-translational activation of aldehyde oxidase and xanthine dehydrogenase by transferring a sulfur atom to the desulfo-molybdenum cofactor of these enzymes. ABA3 is a two-domain protein consisting of an NH(2)-terminal NifS-like cysteine desulfurase domain and a C-terminal domain of yet undescribed function. The NH(2)-terminal domain...
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