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Literature summary for 6.2.1.B11 extracted from

  • Weiße, R.H.; Faust, A.; Schmidt, M.; Schönheit, P.; Scheidig, A.J.
    Structure of NDP-forming Acetyl-CoA synthetase ACD1 reveals a large rearrangement for phosphoryl transfer (2016), Proc. Natl. Acad. Sci. USA, 113, E519-E528.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

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

Organism UniProt Comment Textmining
Candidatus Korarchaeum cryptofilum B1L3C9
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Candidatus Korarchaeum cryptofilum OPF8 B1L3C9
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Synonyms

Synonyms Comment Organism
acyl-CoA synthetase (NDP forming)
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Candidatus Korarchaeum cryptofilum
Kcr_0198
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Candidatus Korarchaeum cryptofilum