Crystallization (Comment) | Organism |
---|---|
crystal structure of a trapped complex of ubiquitin ligase Rsp5 with ubiquitin and substrate Sna3 cytoplasmic domain as a proxy for the catalytic intermediate. The covalent linkage between ubiquitin and the HECT domain is oriented by ubiquitin interactions with the HECT domain N- and C-lobes that stabilize HECT domain conformation. The HECT domain architecture of the ligase primed for ligation prioritizes potential target lysines by their placement relative to a composite catalytic center for ubiquitination | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | P39940 | - |
- |
Saccharomyces cerevisiae ATCC 204508 | P39940 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | ubiquitin ligases HECT E3 use a two-step mechanism to ligate ubiquitin to target proteins. The second step of ligation is mediated by a distinct catalytic architecture established by both the HECT E3 and its covalently linked ubiquitin. There exist three-way interactions between ubiquitin and the bilobal HECT domain orienting the E3-ubiquitin thioester bond for ligation, and restricting the location of the substrate-binding domain to prioritize targets lysines for ubiquitination | Saccharomyces cerevisiae | ? | - |
? | |
additional information | ubiquitin ligases HECT E3 use a two-step mechanism to ligate ubiquitin to target proteins. The second step of ligation is mediated by a distinct catalytic architecture established by both the HECT E3 and its covalently linked ubiquitin. There exist three-way interactions between ubiquitin and the bilobal HECT domain orienting the E3-ubiquitin thioester bond for ligation, and restricting the location of the substrate-binding domain to prioritize targets lysines for ubiquitination | Saccharomyces cerevisiae ATCC 204508 | ? | - |
? | |
[Rsp-ubiquitin-conjugating enzyme UbcH5B]-S-ubiquitin-L-cysteine + [Sna3 cytoplasmic domain]-L-lysine | a specific HECT domain architecture may be important for ubiquitin ligation to Sna3 cytoplasmic domain, which involves both the catalytic C-lobe and the distal N-lobe packing differently from the arrangement promoting ubiquitin transfer from E2 enzyme to E3-ubiquitin intermediate | Saccharomyces cerevisiae | [Rsp5-ubiquitin-conjugating enzyme UbcH5B]-L-cysteine + [Sna3 cytoplasmic domain]-N6-ubiquitinyl-L-lysine | - |
? | |
[Rsp-ubiquitin-conjugating enzyme UbcH5B]-S-ubiquitin-L-cysteine + [Sna3 cytoplasmic domain]-L-lysine | a specific HECT domain architecture may be important for ubiquitin ligation to Sna3 cytoplasmic domain, which involves both the catalytic C-lobe and the distal N-lobe packing differently from the arrangement promoting ubiquitin transfer from E2 enzyme to E3-ubiquitin intermediate | Saccharomyces cerevisiae ATCC 204508 | [Rsp5-ubiquitin-conjugating enzyme UbcH5B]-L-cysteine + [Sna3 cytoplasmic domain]-N6-ubiquitinyl-L-lysine | - |
? |
Synonyms | Comment | Organism |
---|---|---|
RSP5 | - |
Saccharomyces cerevisiae |