CATH Classification

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 D0ZVG2
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.

UniProtKB Entries (2)

D0ZVG2
SSPH1_SALT1
Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S
E3 ubiquitin-protein ligase SspH1
Q16512
PKN1_HUMAN
Homo sapiens
Serine/threonine-protein kinase N1

PDB Structure

PDB 4NKG
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Structure of an SspH1-PKN1 Complex Reveals the Basis for Host Substrate Recognition and Mechanism of Activation for a Bacterial E3 Ubiquitin Ligase.
Keszei, A.F., Tang, X., McCormick, C., Zeqiraj, E., Rohde, J.R., Tyers, M., Sicheri, F.
Mol.Cell.Biol.