1xdf

Crystal structure of pathogenesis-related protein LlPR-10.2A from yellow lupine

spinqualitylabelsall models 1xdf, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1xdf is a 2 chain structure with sequence from Lupinus luteus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: EPE, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P102A_LUPLU Class II ribonuclease (RNase) (By similarity). Binds to cytokinins (By similarity). Interacts with melatonin (By similarity).[UniProtKB:P52779][UniProtKB:Q9LLQ2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 A resolution data. The general fold of LlPR-10.2A resembles that of the other PR-10 proteins and consists of a long C-terminal alpha-helix surrounded by a seven-stranded antiparallel beta-sheet, with two shorter alpha-helices located between strands beta1 and beta2. The most variable part of the structure, the C-terminal helix, is strongly kinked towards the beta-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. Structure of a yellow lupin pathogenesis-related PR-10 protein belonging to a novel subclass.,Pasternak O, Biesiadka J, Dolot R, Handschuh L, Bujacz G, Sikorski MM, Jaskolski M Acta Crystallogr D Biol Crystallogr. 2005 Jan;61(Pt 1):99-107. Epub 2004, Dec 17. PMID:15608381 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA