Crystallographic studies of the coupling segment NBD94674-781 of the nucleotide-binding domain of the Plasmodium yoelii reticulocyte-binding protein Py235

Ardina Grüber, Malathy S.S. Manimekalai, Peter R. Preiser, Gerhard Grüber*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

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 (NBD94444-547), hinge region (NBD94566-663) and C-terminal coupling region (NBD94674-781), and has been proposed to link ATP/ADP binding to the interaction of Py235 with the red blood cell. Here, NBD94674-781 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.

Original languageEnglish
Pages (from-to)1631-1634
Number of pages4
JournalActa Crystallographica Section F: Structural Biology and Crystallization Communications
Volume66
Issue number12
DOIs
Publication statusPublished - Dec 2010
Externally publishedYes

ASJC Scopus Subject Areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Genetics
  • Condensed Matter Physics

Keywords

  • ATP/ADP sensors
  • malaria
  • nucleotide-binding domain
  • Plasmodium

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