5c9y | pdb_00005c9y

Crystal structure of yellow lupine LlPR-10.1A protein partially saturated with trans-zeatin

spinqualitylabelsall models 5c9y, resolution 1.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5c9y is a 1 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 1.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function L18A_LUPLU Publication Abstract from PubMed Plant pathogenesis-related class 10 (PR-10) proteins are a family of abundant proteins initially identified as elements of the plant defense system. The key structural feature suggesting PR-10 functionality is a huge hydrophobic cavity created in the protein interior by a scaffold composed of an extended beta-sheet wrapped around a long and flexible C-terminal alpha-helix. Several crystallographic and NMR studies have shown that the cavity can accommodate a variety of small molecule ligands, including phytohormones. The article describes approximately 1.3A resolution crystal structures of a Lupinus luteus PR-10 isoform LlPR-10.1A, in its free form and in complex with trans-zeatin, a naturally occurring plant hormone belonging to the cytokinin group. Moreover we present the structure of the same protein where the saturation with zeatin is not complete. This set of three crystal structures allows us to track the structural adaptation of the protein upon trans-zeatin docking, as well as the sequence of the ligand-binding events, step-by-step. In addition, titration of LlPR-10.1A with trans-zeatin monitored in solution by CD spectra, confirmed the pattern of structural adaptations deduced from the crystallographic studies. The ligand-biding mode shows no similarity to other zeatin complexes of PR-10 proteins. The present work, which describes the first atomic models of the same PR-10 protein with and without a physiological ligand, reveals that the conformation of LlPR-10.1A undergoes a significant structural rearrangement upon trans-zeatin binding. Crystallographic and CD probing of ligand-induced conformational changes in a plant PR-10 protein.,Sliwiak J, Dolot R, Michalska K, Szpotkowski K, Bujacz G, Sikorski M, Jaskolski M J Struct Biol. 2015 Nov 28. pii: S1047-8477(15)30105-2. doi:, 10.1016/j.jsb.2015.11.008. PMID:26644353 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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