Crystallographic studies of the coupling segment NBD94(674-781) of the nucleotide-binding domain of the Plasmodium yoelii reticulocyte-binding protein Py235.
The Plasmodium yoelii reticulocyte-binding protein Py235 has a role as an ATP/ADP sensor. The sensor domain of Py235 is called NBD94; it consists of at least three functional regions, the nucleotide-binding region (NBD94(444-547)), hinge region (NBD94(566-663)) and C-terminal coupling region (NBD94(674-781)), and has been proposed to link ATP/ADP binding to the interaction of Py235 with the red blood cell. Here, NBD94(674-781) was cloned, expressed and purified to high purity. The monodisperse protein was crystallized by vapour diffusion. A diffraction data set was collected to 2.9 Å resolution with 97.2% completeness using a synchrotron-radiation source. The crystals belonged to space group C2, with unit-cell parameters a=65.08, b=82.71, c=114.27 Å, β=94.72°, and contained four molecules in the asymmetric unit.
Nanyang Technological University, School of Biological Sciences, 60 Nanyang Drive, Singapore 637551, Singapore.
Ardina
A
Grüber
Malathy S S
MS
Manimekalai
Peter R
PR
Preiser
Gerhard
G
Grüber
D018360:Crystallography, X-Ray; D004591:Electrophoresis, Polyacrylamide Gel; D009711:Nucleotides / Q000378:metabolism*; D010967:Plasmodium yoelii / Q000737:chemistry*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D015800:Protozoan Proteins / Q000737:chemistry*; D012156:Reticulocytes / Q000378:metabolism*
D009711:Nucleotides; D015800:Protozoan Proteins