Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1

Taiga Tominaga, Satoshi Watanabe, Rie Matsumi, Haruyuki Atomi, Tadayuki Imanaka, Kunio Miki

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)1153-1157
Number of pages5
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Issue number10
Publication statusPublished - 2012 Oct


  • [NiFe]-hydrogenase maturation proteins
  • HypF
  • Thermococcus kodakarenesis


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