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Literature summary for 2.3.1.169 extracted from

  • Volbeda, A.; Darnault, C.; Tan, X.; Lindahl, P.A.; Fontecilla-Camps, J.C.
    Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica (2009), Biochemistry, 48, 7916-7926.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of a 49 kDa fragment containing residues 311-729 of the intact enzyme and a C-terminal His tag, in Escherichia coli Moorella thermoacetica

Crystallization (Commentary)

Crystallization (Comment) Organism
49 kDa fragment containing residues 311-729 of the intact enzym. In the fragment, domains A2 and A3 have significantlymoved to each other, corresponding to a rotation around a hinge region located close to the C-terminus of the long interdomain helix Moorella thermoacetica
crystal structure of recombinant ACS lacking the N-terminal domain that interacts with carbon monoxide dehydrogenase shows a large reorganization of the remaining two globular domains, producing a narrow cleft of suitable size, shape, and nature to bind CoA. Sequence comparisons with homologous archaeal enzymes that naturally lack the N-terminal domain show that many amino acids lining this cleft are conserved. Besides the typical [4Fe-4S] center, the A-cluster contains only one proximal metal ion that is most likely Cu or Zn. Incorporation of a functional Ni2Fe4S4 A-cluster would require only minor structural rearrangements Moorella thermoacetica

Organism

Organism UniProt Comment Textmining
Moorella thermoacetica
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Moorella thermoacetica P27988
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