3HGF

Expression, purification, spectroscopical and crystallographical studies of segments of the nucleotide binding domain of the reticulocyte binding protein Py235 of Plasmodium yoelii

Summary for 3HGF

• Entry DOI: 10.2210/pdb3hgf/pdb
• Descriptor: Rhoptry protein fragment (1 entity in total)
• Functional Keywords: helix-turn-helix, nucleotide binding protein
• Biological source: Plasmodium yoelii yoelii
• Total number of polymer chains: 3
• Total formula weight: 38606.94

Authors

Gruber, A.,Manimekalai, M.S.S.,Balakrishna, A.M.,Hunke, C.,Jeyakanthan, J.,Preiser, P.R.,Gruber, G. (deposition date: 2009-05-13, release date: 2010-02-23, Last modification date: 2024-03-20)

Primary citation

Gruber, A.,Manimekalai, M.S.S.,Balakrishna, A.M.,Hunke, C.,Jeyakanthan, J.,Preiser, P.R.,Gruber, G.
Structural determination of functional units of the nucleotide binding domain (NBD94) of the reticulocyte binding protein Py235 of Plasmodium yoelii
Plos One, 5:e9146-e9146, 2010

PubMed Abstract: Invasion of the red blood cells (RBC) by the merozoite of malaria parasites involves a large number of receptor ligand interactions. The reticulocyte binding protein homologue family (RH) plays an important role in erythrocyte recognition as well as virulence. Recently, it has been shown that members of RH in addition to receptor binding may also have a role as ATP/ADP sensor. A 94 kDa region named Nucleotide-Binding Domain 94 (NBD94) of Plasmodium yoelii YM, representative of the putative nucleotide binding region of RH, has been demonstrated to bind ATP and ADP selectively. Binding of ATP or ADP induced nucleotide-dependent structural changes in the C-terminal hinge-region of NBD94, and directly impacted on the RBC binding ability of RH.

PubMed: 20161776
DOI: 10.1371/journal.pone.0009146

Experimental method

X-RAY DIFFRACTION (4 Å)