Crystallization (Comment) | Organism |
---|---|
purified ckcACD1 enzyme in complex with phosphorylated His254alpha and in complex with ADP or with the nonhydrolyzable ATP analogue AMPPCP, X-ray diffraction structure determination and analysis at 1.9-2.4 A resolution | Candidatus Korarchaeum cryptofilum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | required | Candidatus Korarchaeum cryptofilum | |
additional information | the metal ion is coordinated by the side chain of Asp351alpha' | Candidatus Korarchaeum cryptofilum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + acetate + CoA | Candidatus Korarchaeum cryptofilum | - |
ADP + phosphate + acetyl-CoA | - |
r |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Candidatus Korarchaeum cryptofilum | B1L3C9 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation of His254, conformation of the phosphorylated His is stabilized by ionic interaction with the side-chain carboxyl group of Glu213alpha, a hydrogen bridge provides an ideal geometry for the phosphorylation reaction by favoring the protonation state of the imidazole group. In addition, the phosphoryl moiety forms a hydrogen bond to the hydroxyl group of Ser160alpha. In the crystal structure ckcACD1-H, the phosphate moiety also interacts with a bound metal ion | Candidatus Korarchaeum cryptofilum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + acetate + CoA | - |
Candidatus Korarchaeum cryptofilum | ADP + phosphate + acetyl-CoA | - |
r | |
additional information | 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, binding mode of the Ac moiety within acetyl-CoA, and binding mode of Ado nucleotides within site II located in the beta subunit | Candidatus Korarchaeum cryptofilum | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
heterotetramer | unique arrangement of the ACD subunits alpha and beta within an alpha2beta2-heterotetrameric complex | Candidatus Korarchaeum cryptofilum |
More | overall structure and domain arrangement of ckcACD1, overview | Candidatus Korarchaeum cryptofilum |
Synonyms | Comment | Organism |
---|---|---|
ACD | - |
Candidatus Korarchaeum cryptofilum |
ckcACD1 | - |
Candidatus Korarchaeum cryptofilum |
NDP-forming acyl-CoA synthetase | - |
Candidatus Korarchaeum cryptofilum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
ATP | - |
Candidatus Korarchaeum cryptofilum |
General Information | Comment | Organism |
---|---|---|
evolution | the ACD enzymes are considered to be primordial enzymes of ATP synthesis in the early evolution of life. The structure reveals a unique arrangement of the ACD subunits alpha and beta within an alpha2beta2-heterotetrameric complex. This arrangement significantly differs from other members of the superfamily. Residues Ser160alpha and Asp351alpha' are highly conserved throughout the ACD superfamily | Candidatus Korarchaeum cryptofilum |
physiological function | the NDP-forming acyl-CoA synthetases (ACDs) catalyze the conversion of various CoA thioesters to the corresponding acids, conserving their chemical energy in form of ATP. The ACDs are the major energy-conserving enzymes in sugar and peptide fermentation of hyperthermophilic archaea | Candidatus Korarchaeum cryptofilum |