Structure of the [NiFe] Hydrogenase Maturation Protein HypF from Thermococcus kodakaraensis KOD1
Structure of the [NiFe] Hydrogenase Maturation Protein HypF from Thermococcus kodakaraensis KOD1
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来自 Thermococcus kodakaraensis KOD1 的 [NiFe] 氢化酶成熟蛋白 HypF 的结构
DOI：
10.1107/s1744309112036421
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发表时间：
2012
期刊：
影响因子：
--
通讯作者：
and K. Miki
中科院分区：
文献类型：
--
作者：
T. Tominaga;S. Watanabe;R. Matsumi;H. Atomi;T. Imanaka;and K. Miki
HypF参与了[NiFe]-氢化酶的NiFe(CN)2CO中心的CN配体的生物合成。本文以4.5 Å分辨率报道了柯达arenesis热球菌的HypF全长结构。n端酰基磷酸酶样（ACP）结构域与锌指结构域相互作用，其相对位置具有一定的灵活性。分子表面分析表明，在ACP和锌指结构域之间形成的深口袋是高度保守的，具有正电位。这些结果表明，所鉴定的带正电荷的口袋参与了氨甲酰磷酸的水解和氨甲酰中间体的形成。
HypF is involved in the biosynthesis of the CN ligand of the NiFe(CN)2CO centre of [NiFe]-hydrogenases. Here, the full-length structure of HypF from Thermococcus kodakarenesis is reported at 4.5 Å resolution. The N-terminal acylphosphatase-like (ACP) domain interacts with the zinc-finger domain with some flexibility in its relative position. Molecular-surface analysis shows that a deep pocket formed between the ACP and zinc-finger domains is highly conserved and has positive potential. These results suggest that the positively charged pocket identified is involved in the hydrolysis of carbamoyl phosphate and the formation of a carbamoyl intermediate.