Structure of a yellow lupin pathogenesis-related PR-­10 protein belonging to a novel subclass

Pathogenesis-related (PR) proteins of class 10 are abundant in higher plants. Some of these proteins are induced under stress conditions as part of the plant defence mechanism. Other homologues are developmentally regulated and their expression varies in different plant organs. The PR-10 proteins are encoded by multigene families, have a weight of about 17 kDa and are found in the cytosol. In yellow lupin, nine different homologues have been identified and divided into two subclasses, LlPR-10.1 and LlPR-10.2. Within each subclass the sequence identity is about 75–91%, while across the subclasses it is only 59–60%. Here, the crystal structure of a yellow lupin PR-10 protein from the second subclass, LlPR-­10.2A, is presented. The structure was solved by molecular replacement and refined to R = 0.205 using 1.9 Å resolution data. The general fold of LlPR-10.2A resembles that of the other PR-10 proteins and consists of a long C-­terminal α-helix surrounded by a seven-stranded antiparallel β-sheet, with two shorter α-helices located between strands β1 and β2. The most variable part of the structure, the C-terminal helix, is strongly kinked towards the β-sheet core in both LlPR-10.2A molecules present in the asymmetric unit. This unexpected feature reduces the size of the hydrophobic cavity observed in other PR-10 proteins that is reported to be the ligand-binding site. As in other PR-10 structures, a surface loop located near the entrance to the cavity shows very high structural conservation and stability despite the high glycine content in its sequence.