title: Structure of the [NiFe]-hydrogenase maturation protein HypF from Thermococcus kodakarensis KOD1.
abstract: HypF is involved in the biosynthesis of the CN ligand of the NiFe(CN)(2)CO 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.
authors.affiliation: Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
authors.forename: Taiga
authors.initials: T
authors.lastname: Tominaga
authors.forename: Satoshi
authors.initials: S
authors.lastname: Watanabe
authors.forename: Rie
authors.initials: R
authors.lastname: Matsumi
authors.forename: Haruyuki
authors.initials: H
authors.lastname: Atomi
authors.forename: Tadayuki
authors.initials: T
authors.lastname: Imanaka
authors.forename: Kunio
authors.initials: K
authors.lastname: Miki
mesh_terms: D019878:Carboxyl and Carbamoyl Transferases / Q000737:chemistry*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D019712:Thermococcus / Q000201:enzymology*
chemical_list: D019878:Carboxyl and Carbamoyl Transferases