Open AccessCrystallographic studies of the coupling segment NBD94 674–781 of the nucleotide‐binding domain of the Plasmodium yoelii reticulocyte‐binding protein Py235
Author(s) -
Grüber Ardina,
Manimekalai Malathy S. S.,
Preiser Peter R.,
Grüber Gerhard
Publication year - 2010
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309110040996
Subject(s) - crystallography , reticulocyte , nucleotide , cyclic nucleotide binding domain , chemistry , biology , biochemistry , rna , gene
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 C 2, 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.