Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.

@article{Rosano2002CrystalSA,
  title={Crystal structure and anion binding in the prokaryotic hydrogenase maturation factor HypF acylphosphatase-like domain.},
  author={C. Rosano and S. Zuccotti and M. Bucciantini and M. Stefani and G. Ramponi and M. Bolognesi},
  journal={Journal of molecular biology},
  year={2002},
  volume={321 5},
  pages={
          785-96
        }
}
[NiFe]-hydrogenases require a set of complementary and regulatory proteins for correct folding and maturation processes. One of the essential regulatory proteins, HypF (82kDa) contains a N-terminal acylphosphatase (ACT)-like domain, a sequence motif shared with enzymes catalyzing O-carbamoylation, and two zinc finger motifs similar to those found in the DnaJ chaperone. The HypF acylphosphatase domain is thought to support the conversion of carbamoylphosphate into CO and CN(-), promoting… Expand
Structure of hydrogenase maturation protein HypF with reaction intermediates shows two active sites.
Hydrogenase Maturation Protein HypF
Structure of [NiFe] hydrogenase maturation protein HypE from Escherichia coli and its interaction with HypF.
Crystallization and preliminary X-ray crystallographic analysis of the [NiFe]-hydrogenase maturation factor HypF1 from Ralstonia eutropha H16.
Structural Basis for the Reaction Mechanism of S-Carbamoylation of HypE by HypF in the Maturation of [NiFe]-Hydrogenases*
Structural diversity in twin-arginine signal peptide-binding proteins
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