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Literature summary for 2.3.2.27 extracted from

  • Plechanovova, A.; Jaffray, E.G.; Tatham, M.H.; Naismith, J.H.; Hay, R.T.
    Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis (2012), Nature, 489, 115-120.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

Crystallization (Comment) Organism
isoform Rnf4 trimeric complex with UbcH5a and ubiquitin. E2 enzyme UbcH5a is linked by an isopeptide bond to ubiquitin. UbcH5a contacts a single protomer of the RING, and ubiquitin is folded back onto the UbcH5a by contacts from both RING protomers. The C-terminal tail of ubiquitin is locked into an active site groove on UbcH5a by an intricate network of interactions, resulting in changes at the UbcH5a active site Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus O88846
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Synonyms

Synonyms Comment Organism
RNF4
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Rattus norvegicus