1ifv | pdb_00001ifv

CRYSTAL STRUCTURE OF PATHOGENESIS-RELATED PROTEIN LLPR10.1B FROM YELLOW LUPINE

spinqualitylabelsall models 1ifv, resolution 2.25Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ifv is a 2 chain structure with sequence from European yellow lupin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1btv, 1b6f, 1icx Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [L18B_LUPLU] Class II ribonuclease (RNase), with low activity on single-strand RNA. 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 class 10 (PR10) proteins are restricted to the plant kingdom where they are coded by multigene families and occur at high levels. In spite of their abundance, their physiological role is obscure although members of a distantly related subclass (cytokinin-specific binding proteins) are known to bind plant hormones. PR10 proteins are of special significance in legume plants where their expression patterns are related to infection by the symbiotic, nitrogen-fixing bacteria. Here we present the first crystal structures of classic PR10 proteins representing two homologues from one subclass in yellow lupine. The general fold is similar and, as in a birch pollen allergen, consists of a seven-stranded beta-sheet wrapped around a long C-terminal helix. The mouth of a large pocket formed between the beta-sheet and the helix seems a likely site for ligand binding. The shape of the pocket varies because, in variance with the rigid beta-sheet, the helix shows unusual conformational variability consisting in bending, disorder, and axial shifting. A surface loop, proximal to the entrance to the internal cavity, shows an unusual structural conservation and rigidity in contrast to the high glycine content in its sequence. The loop is different from the so-called glycine-rich P-loops that bind phosphate groups of nucleotides, but it is very likely that it does play a role in ligand binding in PR10 proteins. Crystal structures of two homologous pathogenesis-related proteins from yellow lupine.,Biesiadka J, Bujacz G, Sikorski MM, Jaskolski M J Mol Biol. 2002 Jun 21;319(5):1223-34. PMID:12079359 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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