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.
|ジャーナル||Acta Crystallographica Section F: Structural Biology and Crystallization Communications|
|出版ステータス||Published - 2012 10|
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