Crystallization (Comment) | Organism |
---|---|
arrangement of the acyl-CoA synthetase subunits alpha and beta within an alpha2beta2-heterotetrameric complex significantly differs from other members of the superfamily. To transmit an activated phosphoryl moiety from the acetyl-CoA binding site (within the alpha subunit) to the NDP-binding site (within the beta subunit), a distance of 51 A has to be bridged. This transmission requires a larger rearrangement within the protein complex involving a 21-aa-long phosphohistidine-containing segment of the alpha subunit. Spatial restraints of the interaction of this segment with the beta subunit explain the necessity for a second highly conserved His residue within the beta subunit | Candidatus Korarchaeum cryptofilum |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candidatus Korarchaeum cryptofilum | B1L3C9 | - |
- |
Candidatus Korarchaeum cryptofilum OPF8 | B1L3C9 | - |
- |
Synonyms | Comment | Organism |
---|---|---|
acyl-CoA synthetase (NDP forming) | - |
Candidatus Korarchaeum cryptofilum |
Kcr_0198 | - |
Candidatus Korarchaeum cryptofilum |