1AYZ

CRYSTAL STRUCTURE OF THE SACCHAROMYCES CEREVISIAE UBIQUITIN-CONJUGATING ENZYME RAD6 (UBC2) AT 2.6A RESOLUTION

Summary for 1AYZ

• Entry DOI: 10.2210/pdb1ayz/pdb
• Descriptor: UBIQUITIN-CONJUGATING ENZYME RAD6 (2 entities in total)
• Functional Keywords: ubiquitin conjugation, ubiquitin-conjugating enzyme
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: P06104
• Total number of polymer chains: 3
• Total formula weight: 58092.87

Authors

Worthylake, D.K.,Prakash, S.,Prakash, L.,Hill, C.P. (deposition date: 1997-11-12, release date: 1998-08-26, Last modification date: 2024-05-22)

Primary citation

Worthylake, D.K.,Prakash, S.,Prakash, L.,Hill, C.P.
Crystal structure of the Saccharomyces cerevisiae ubiquitin-conjugating enzyme Rad6 at 2.6 A resolution.
J.Biol.Chem., 273:6271-6276, 1998

PubMed Abstract: 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 active site cysteine lies in a cleft formed by a coil region that includes the 310 helix and a loop that is in different conformations for the three molecules in the asymmetric unit. Residues important for Rad6 interaction with Ubr1 and Rad18 are on the opposite side of the structure from the active site, indicating that this part of the UBC surface participates in protein-protein interactions that define Rad6 substrate specificity.

PubMed: 9497353
DOI: 10.1074/jbc.273.11.6271

Experimental method

X-RAY DIFFRACTION (2.6 Å)