Literature summary for 2.3.2.31 extracted from

Yuan, L.; Lv, Z.; Atkison, J.; Olsen, S.
Structural insights into the mechanism and E2 specificity of the RBR E3 ubiquitin ligase HHARI (2017), Nat. Commun., 8, 211 .

Cloned(Commentary)

Cloned (Comment)	Organism
-	Homo sapiens

Crystallization (Commentary)

Crystallization (Comment)	Organism
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	Homo sapiens

Crystallization (Comment)

Organism

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

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	Q9Y4X5	-	-

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Release 2023.1 (January 2023)