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

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

研究成果: Article査読

10 被引用数 (Scopus)

抄録

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.

本文言語English
ページ(範囲)1153-1157
ページ数5
ジャーナルActa Crystallographica Section F: Structural Biology and Crystallization Communications
68
10
DOI
出版ステータスPublished - 2012 10
外部発表はい

ASJC Scopus subject areas

  • 生物理学
  • 構造生物学
  • 生化学
  • 遺伝学
  • 凝縮系物理学

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