Structural basis for the preference of the Arabidopsis thalianaphosphatase RLPH2 for tyrosine-phosphorylated substrates.

Calcineurin-like metallo-phosphoesterase superfamily protein, Putative uncharacterized protein At3g09970,Putative uncharacterized protein T22K18.22

MAQKPRTVICVGDIHGYISKLNNLWLNLQSAIDPSDFSSALVIFLGDYCDRGPETRKVIDFLISLPEKHPDQTHVFLAGN
HDFAFSGFLGLLPRPSDGSDLKDTWKEYSKSEETEGWYTGEGFEDMHLQGRRWAGKIKATFNSVKGMAYKGSIYDAGSTF
ESYGVPHGSSDLMKAVPESHKKFLTNMVWVHEEDDVCIETEEGLKHCKLIAVHAGLEKGNNVEEQLKLLRAKDTSISKIQ
HLSGRKNVWDIPQELDDKHTVVVSGHHGKLHIDGMRLIIDEGGGFPDKPVAAIVLPSKKIIRDTDNLSS

100 mM Bis-Tris-Cl, 250 g/L PEG 3350, 200 g/L glycerol

Natural Sciences and Engineering Research Council (NSERC, Canada)

protein phosphorylation, Arabidopsis thaliana, Phosphoprotein phosphatase, protein phosphatase, protein tyrosine phosphatase, HYDROLASE