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1ayz
From Proteopedia
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[[Category: ubiquitin-conjugating enzyme]] | [[Category: ubiquitin-conjugating enzyme]] | ||
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Revision as of 12:48, 30 October 2007
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CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE UBIQUITIN-CONJUGATING ENZYME RAD6 (UBC2) AT 2.6A RESOLUTION
Overview
The Saccharomyces cerevisiae ubiquitin-conjugating enzyme (UBC) Rad6 is, required for several functions, including the repair of UV damaged DNA, damage-induced mutagenesis, sporulation, and the degradation of cellular, proteins that possess destabilizing N-terminal residues. Rad6 mediates its, role in N-end rule-dependent protein degradation via interaction with the, ubiquitin-protein ligase Ubr1 and in DNA repair via interactions with the, DNA binding protein Rad18. We report here the crystal structure of Rad6, refined at 2.6 A resolution to an R factor of 21.3%. The protein adopts an, alpha/beta fold that is very similar to other UBC structures. An apparent, difference at the functionally important first helix, however, has, prompted a reassessment of previously reported structures. The ... [(full description)]
About this Structure
1AYZ is a [Single protein] structure of sequence from [Saccharomyces cerevisiae]. Active as [Ubiquitin--protein ligase], with EC number [6.3.2.19]. Structure known Active Site: NUL. Full crystallographic information is available from [OCA].
Reference
Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 A resolution., Worthylake DK, Prakash S, Prakash L, Hill CP, J Biol Chem. 1998 Mar 13;273(11):6271-6. PMID:9497353
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