1FZY

CRYSTAL STRUCTURE OF SACCHAROMYCES CEREVISIAE UBIQUITIN CONJUGATING ENZYME 1

Summary for 1FZY

• Entry DOI: 10.2210/pdb1fzy/pdb
• Descriptor: UBIQUITIN-CONJUGATING ENZYME E2-24 KDA (2 entities in total)
• Functional Keywords: alpha-beta roll, ligase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 33394.13

Authors

Glover, M.,Williams, R.S. (deposition date: 2000-10-04, release date: 2001-10-04, Last modification date: 2024-02-07)

Primary citation

Hamilton, K.S.,Ellison, M.J.,Barber, K.R.,Williams, R.S.,Huzil, J.T.,McKenna, S.,Ptak, C.,Glover, M.,Shaw, G.S.
Structure of a conjugating enzyme-ubiquitin thiolester intermediate reveals a novel role for the ubiquitin tail.
Structure, 9:897-904, 2001

PubMed Abstract: Ubiquitin-conjugating enzymes (E2s) are central enzymes involved in ubiquitin-mediated protein degradation. During this process, ubiquitin (Ub) and the E2 protein form an unstable E2-Ub thiolester intermediate prior to the transfer of ubiquitin to an E3-ligase protein and the labeling of a substrate for degradation. A series of complex interactions occur among the target substrate, ubiquitin, E2, and E3 in order to efficiently facilitate the transfer of the ubiquitin molecule. However, due to the inherent instability of the E2-Ub thiolester, the structural details of this complex intermediate are not known.

PubMed: 11591345
DOI: 10.1016/S0969-2126(01)00657-8

Experimental method

X-RAY DIFFRACTION (1.9 Å)