2.3.2.31: RBR-type E3 ubiquitin transferase
This is an abbreviated version!
For detailed information about RBR-type E3 ubiquitin transferase, go to the full flat file.
Word Map on EC 2.3.2.31
Reaction
Synonyms
ARIH1, ARIH2, HHARI, HOIP, Parkin, parkin RBR E3 ubiquitin ligase, PRKN, RBR E3, RBR-type E3, RBR-type E3 ligase, RBX1, RFA1, RFA4, RING Finger ABA-Related, RNF144, RNF144A, RNF144AA, RNF144AB, RNF144B, RNF19A, RNF19B, RNF217, RNF31, Triad1
ECTree
2.3.2.31 RBR-type E3 ubiquitin transferaseAdvanced search results
results (
results (Crystallization
Crystallization on EC 2.3.2.31 - RBR-type E3 ubiquitin transferase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
CRYSTALLIZATION (Commentary) 
ORGANISM
UNIPROT
LITERATURE
cocrystal structure of HOIP RBR domain with single-domain antibody, use as a platform for soaking of ligands that target the active site cysteine of HOIP
structure of a parkin-phosphoubiquitin complex. Phosphoubiquitin binding induces a movement in the IBR domain to reveal a cryptic ubiquitin binding site. Mutation of this site negatively impacts on Parkin's activity. Ubiquitin binding promotes cooperation between parkin molecules
structure of ARIH1 in complex with UbcH7-ubiquitin, to 3.2 A resolution. ARIH1 is autoinhibited even in the complex. The ARIH1 UBA-L domain binds to ubiquitin and NEDD8
structure of isoform HHARI, in complex with a UbcH7-ubiquitin thioester mimetic. Mechanistically important conformational changes in the RING1 and UBA-like domains of HHARI accompany UbcH7-ubiquitin binding. HHARI recruits E2-ubiquitin in an open conformation. HHARI optimally functions with UbcH7 that solely performs transthiolation, and HHARI prevents spurious discharge of ubiquitin from E2 to lysine residues by harboring structural elements that block E2-ubiquitin from adopting a closed conformation and participating in contacts to ubiquitin that promote an open E2-ubiquitin conformation
structure of the fully active HOIP-RBR in its transfer complex with an E2-ubiquitin conjugate. HOIP-RBR binds the E2-ubiquitin conjugate in an elongated fashion, with the E2 and E3 catalytic centers aligned for ubiquitin transfer, which structurally both requires and enables a HECT-like mechanism. Three distinct helix-IBR-fold motifs form ubiquitin-binding regions that engage the activated ubiquitin of the E2-ubiquitin conjugate as well as an additional regulatory ubiquitin molecule
