Crystallization and preliminary X-ray diffraction study of the histidine-containing phosphotransfer protein ZmHP1 from maize.
In histidine-aspartate phosphorelays (two-component systems) involved in plant-hormone signalling, histidine-containing phosphotransfer (HPt) proteins mediate the transfer of a phosphoryl group from the sensory histidine kinase to the response regulator. The maize HPt protein ZmHP1 has been crystallized. Although ZmHP1 with an N-terminal His tag could be crystallized using sodium chloride as a precipitant, the crystals diffracted poorly to only 3.2 A resolution. When the His tag was removed, ZmHP1 crystals were obtained using polyethylene glycol 4000 as a precipitant and the diffraction data were greatly enhanced to 2.4 A resolution. The crystals belonged to the space group P4(1)2(1)2, with one ZmHP1 molecule in the asymmetric unit.
Sugawara
Hajime
H
Laboratory for Communication Mechanisms, RIKEN Plant Science Center, Yokohama 230-0045, Japan. sugawara@psc.riken.go.jp
Yamaya
Tomoyuki
T
Sakakibara
Hitoshi
H
D003001:Cloning, Molecular / Q000379:methods; D003460:Crystallization / Q000379:methods; D006639:Histidine / Q000737:chemistry*; D017853:Phosphotransferases (Alcohol Group Acceptor) / Q000737:chemistry*; D010940:Plant Proteins / Q000737:chemistry*; D011092:Polyethylene Glycols; D014961:X-Ray Diffraction; D003313:Zea mays / Q000737:chemistry*
D010940:Plant Proteins; D011092:Polyethylene Glycols; D006639:Histidine; D017853:Phosphotransferases (Alcohol Group Acceptor)