1FXT
STRUCTURE OF A CONJUGATING ENZYME-UBIQUITIN THIOLESTER COMPLEX
Summary for 1FXT
| Entry DOI | 10.2210/pdb1fxt/pdb |
| Descriptor | UBIQUITIN-CONJUGATING ENZYME E2-24 KDA, UBIQUITIN (2 entities in total) |
| Functional Keywords | model of the interaction between yeast ubc1 and ubiquitin after the formation of a covalent thiolester, ligase |
| Biological source | Saccharomyces cerevisiae (baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 25273.89 |
| Authors | Hamilton, K.S.,Shaw, G.S.,Williams, R.S.,Huzil, J.T.,McKenna, S.,Ptak, C.,Glover, M.,Ellison, M.J. (deposition date: 2000-09-26, release date: 2001-10-10, Last modification date: 2024-05-22) |
| 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 Cited by 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: 11591345DOI: 10.1016/S0969-2126(01)00657-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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