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Structure of the [NiFe]‐hydrogenase maturation protein HypF from

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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.
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Document Type: Research Article

Publication date: 2012-10-01

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