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Crystallization and preliminary X‐ray crystallographic analysis of the extracellular domain of LePRK2 from Lycopersicon esculentum
Author(s) -
Xu Anbi,
Huang Laiqiang
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14000053
Subject(s) - lycopersicon , extracellular , leucine rich repeat , pollen , protein kinase domain , biology , microbiology and biotechnology , kinase , receptor , signal transduction , crystallography , botany , chemistry , biochemistry , gene , mutant
The tomato ( Lycopersicon esculentum ) pollen‐specific receptor kinase 2 (LePRK2) is a member of the large receptor‐like kinase (RLK) family and is expressed specifically in mature pollen and pollen tubes in L. esculentum . Like other RLKs, LePRK2 contains a characteristic N‐terminal leucine‐rich repeat (LRR) extracellular domain, the primary function of which is in protein–protein interactions. The LePRK2 LRR is likely to bind candidate ligands from the external environment, leading to a signal transduction cascade required for successful pollination. LePRK2‐LRR was purified using an insect‐cell secretion expression system and was crystallized using the vapour‐diffusion method. The crystals diffracted to a resolution of 2.50 Å and belonged to space group I 4 1 22, with unit‐cell parameters a = b = 93.94, c = 134.44 Å and one molecule per asymmetric unit.