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

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

doi:10.1107/S1744309112036421

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 journal › Article › peer-review

10 Citations (Scopus)

Abstract

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 language	English
Pages (from-to)	1153-1157
Number of pages	5
Journal	Acta Crystallographica Section F: Structural Biology and Crystallization Communications
Volume	68
Issue number	10
DOIs	https://doi.org/10.1107/S1744309112036421
Publication status	Published - Oct 2012
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biophysics
Structural Biology
Biochemistry
Genetics
Condensed Matter Physics

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abstract = "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 {\AA} 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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T1 - Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1

AU - Tominaga, Taiga

AU - Watanabe, Satoshi

AU - Matsumi, Rie

AU - Atomi, Haruyuki

AU - Imanaka, Tadayuki

AU - Miki, Kunio

PY - 2012/10

Y1 - 2012/10

N2 - 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.

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

Abstract

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