Purification, crystallization and preliminary crystallographic studies of the ligand-binding domain of a plant vacuolar sorting receptor.
Vacuolar sorting receptor (VSR) proteins bind soluble protein ligands in a sequence-specific manner and target them to the lytic vacuole in plant cells. A VSR from Arabidopsis thaliana, AtBP80b, has been successfully purified after heterologous expression in Drosophila S2 cells. The AtBP80b protein (560 amino acids) was crystallized by the hanging-drop method with a PEG 400-based precipitant. Preliminary X-ray diffraction studies of an AtBP80b crystal showed that it belongs to the cubic space group P2(1)3 (or P4(2)32) and has unit-cell parameters a = b = c = 145.9 A. Crystals of the VSR diffract beyond 2.5 A resolution.
Rogers
Sally W
SW
Institute of Biological Chemistry, Washington State University, Pullman, WA 99164-6340, USA.
Youn
Buhyum
B
Rogers
John C
JC
Kang
Chulhee
C
D000818:Animals; D017360:Arabidopsis / Q000737:chemistry*; D029681:Arabidopsis Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*; D001665:Binding Sites; D002460:Cell Line; D003460:Crystallization; D018360:Crystallography, X-Ray; D004330:Drosophila / Q000235:genetics; D008024:Ligands; D017434:Protein Structure, Tertiary; D033921:Vesicular Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism*
D029681:Arabidopsis Proteins; C500310:BP80b protein, Arabidopsis; D008024:Ligands; D033921:Vesicular Transport Proteins