Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica.

Novel domain arrangement in the crystal structure of a truncated acetyl-CoA synthase from Moorella thermoacetica.
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来自热乙酸摩尔菌的截短的乙酰辅酶A合酶晶体结构中的新结构域排列。

DOI:
10.1021/bi9003952
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发表时间:
2009
期刊:
影响因子:
2.9
通讯作者:
Fontecilla-Camps,JuanC
Fontecilla-Camps,JuanC
中科院分区:
生物学3区
文献类型:
--
作者:
Volbeda,Anne;Darnault,Claudine;Tan,Xiangshi;Lindahl,PaulA;Fontecilla-Camps,JuanC

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Ni-dependent acetyl-CoA synthase (ACS) and CO dehydrogenase (CODH) constitute the central enzyme complex of the Wood−Ljungdahl pathway of acetyl-CoA formation. The crystal structure of a recombinant bacterial ACS lacking the N-terminal domain that interacts with CODH 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, according to anomalous scattering data, is most likely Cu or Zn. Incorporation of a functional Ni2Fe4S4A-cluster would require only minor structural rearrangements. Using available structures, a plausible model of the interaction between CODH and the smaller ACS in archaeal multienzyme complexes is presented, along with a discussion of evolutionary relationships of the archaeal and bacterial enzymes.
平衡透析研究以及辅酶 A 与热乙酸梭菌乙酰辅酶 A 合酶/一氧化碳脱氢酶结合的机制意义。
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