PMID:11856843
| Citation |
Rosano, C, Zuccotti, S, Stefani, M, Bucciantini, M, Ramponi, G and Bolognesi, M (2002) Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF. Acta Crystallogr. D Biol. Crystallogr. 58:524-5 |
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| Abstract |
Maturation of prokaryotic hydrogenase involves several protein factors, among which is the accessory protein HypF, which hosts the consensus sequence of acylphosphatases and a sequence motif common to proteins catalyzing O-carbamoylations. The specific functions of HypF are largely unknown, although it has been observed that CN(-) and CO ligands at the hydrogenase Ni,Fe active centre originate from carbamoylphosphate. The HypF N-terminal domain (91 residues, acylphosphatase-like domain) has been crystallized in two different crystal forms belonging to the orthorhombic P2(1)2(1)2(1) space group (unit-cell parameters a = 35.5, b = 59.8, c = 87.6 A) and to the rhombohedral space group R32 (unit-cell parameters a = b = 58.1, c = 155.6 A in the hexagonal setting). |
| Links | |
| Keywords |
Acid Anhydride Hydrolases/chemistry; Amino Acid Sequence; Bacterial Proteins/chemistry; Cloning, Molecular; Crystallization; Crystallography, X-Ray; Escherichia coli/chemistry; Molecular Sequence Data; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid |
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