Crystallization and preliminary X-ray analysis of inorganic polyphosphate/ATP-glucomannokinase from Arthrobacter sp. strain KM.
Inorganic polyphosphate [poly(P)]/ATP-glucomannokinase from Arthrobacter sp. strain KM phosphorylates glucose and mannose, utilizing both ATP and poly(P) as phosphoryl donors. The enzyme was overexpressed in Escherichia coli, purified and crystallized by means of the hanging-drop vapour-diffusion method with ammonium sulfate as the precipitant. The crystals were orthorhombic and belonged to space group P2(1)2(1)2(1), with unit-cell parameters a = 66.2, b = 83.7, c = 103.8 A. Assuming two molecules per asymmetric unit, V(sol) is 0.49. X-ray diffraction data to 2.83 A have been collected from a single crystal.
Mukai
Takako
T
Department of Basic and Applied Molecular Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Kyoto 611-0011, Japan.
Kawai
Shigeyuki
S
Mori
Shigetarou
S
Mikami
Bunzo
B
Murata
Kousaku
K
D001173:Arthrobacter / Q000201:enzymology*; D003001:Cloning, Molecular / Q000379:methods; D003460:Crystallization / Q000379:methods*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014961:X-Ray Diffraction
D017853:Phosphotransferases (Alcohol Group Acceptor); C485979:polyphosphate ATP-glucomannokinase