Crystal Structure and Anion Binding in the Prokaryotic Hydrogenase Maturation Factor HypF Acylphosphatase-like Domain

[NiFe]-hydrogenases require a set of complementary and regulatory proteins for correct folding and maturation processes. One of the essential regulatory proteins, HypF (82 kDa) contains a N-terminal acylphosphatase (ACT)-like domain, a sequence motif shared with enzymes catalyzing O-carbamoylation,...

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Veröffentlicht in:	Journal of molecular biology 2002-08, Vol.321 (5), p.785-796
Hauptverfasser:	Rosano, Camillo, Zuccotti, Simone, Bucciantini, Monica, Stefani, Massimo, Ramponi, Giampietro, Bolognesi, Martino
Format:	Artikel
Sprache:	eng
Schlagworte:	Acid Anhydride Hydrolases - chemistry ACT domains Acylphosphatase acylphosphatase-like structure Amino Acid Sequence Animals Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Cattle Crystallography, X-Ray HypF N-terminal domain Models, Molecular Molecular Sequence Data phosphate loop Phosphates - metabolism Phosphoric Monoester Hydrolases - chemistry Phosphoric Monoester Hydrolases - metabolism Protein Binding Protein Structure, Tertiary Sequence Alignment Sulfates - metabolism X-ray crystallography
Online-Zugang:	Volltext
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