CATH Classification
Level | CATH Code | Description |
---|---|---|
3 | Alpha Beta | |
3.80 | Alpha-Beta Horseshoe | |
3.80.10 | Leucine-rich repeat, LRR (right-handed beta-alpha superhelix) | |
3.80.10.10 | Ribonuclease Inhibitor |
Domain Context
CATH Clusters
Superfamily | Ribonuclease Inhibitor |
Functional Family | Probable E3 ubiquitin-protein ligase ipaH7.8 |
Enzyme Information
2.3.2.27 |
RING-type E3 ubiquitin transferase.
based on mapping to UniProt Q8VSC3
S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
-!- RING E3 ubiquitin transferases serve as mediators bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) and an acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon-amino group of an L-lysine residue of the acceptor protein. -!- Unlike EC 2.3.2.26 the RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin. -!- Many members of the RING-type E3 ubiquitin transferase family are not able to bind a substrate directly, and form a complex with a cullin scaffold protein and a substrate recognition module (the complexes are named CRL for Cullin-RING-Ligase). -!- In these complexes, the RING-type E3 ubiquitin transferase provides an additional function, mediating the transfer of a NEDD8 protein from a dedicated E2 carrier to the cullin protein (see EC 2.3.2.32). -!- Cf. EC 2.3.2.31.
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UniProtKB Entries (1)
Q8VSC3 |
IPA9_SHIFL
Shigella flexneri
E3 ubiquitin-protein ligase ipaH9.8
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PDB Structure
PDB | 5B0T |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structure of the substrate-recognition domain of the Shigella E3 ligase IpaH9.8
Acta Crystallogr.,Sect.F
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