Crystallization and preliminary X-ray characterization of the acylphosphatase-like domain from the Escherichia coli hydrogenase maturation factor HypF.
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).
Rosano
Camillo
C
Advanced Biotechnology Center--IST, Largo Rosanna Benzi 10, 16132 Genoa, Italy.
Zuccotti
Simone
S
Stefani
Massimo
M
Bucciantini
Monica
M
Ramponi
Giampietro
G
Bolognesi
Martino
M
D017766:Acid Anhydride Hydrolases / Q000737:chemistry; D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry*; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017386:Sequence Homology, Amino Acid; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D001426:Bacterial Proteins; D000097024:Acylphosphatase; C108878:HypF protein, Bacteria