3e85

Crystal Structure of Pathogenesis-related Protein LlPR-10.2B from yellow lupine in complex with DiphenylureaCrystal Structure of Pathogenesis-related Protein LlPR-10.2B from yellow lupine in complex with Diphenylurea

Structural highlights 3e85 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 1.95Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function P102B_LUPLU Class II ribonuclease (RNase) (By similarity). Binds to several cytokinins including natural adenine-type (e.g. trans-zeatin and kinetin) and artificial urea-type (e.g. N,N'-diphenylurea and N-phenyl-N'-(2-chloro-4-pyridyl)urea) hormones (PubMed:18406424, PubMed:19220853, PubMed:29630775). Interacts with melatonin (PubMed:29630775).[UniProtKB:P52779] 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 Plant pathogenesis-related (PR) proteins of class 10 are the only group among the 17 PR protein families that are intracellular and cytosolic. Sequence conservation and the wide distribution of PR-10 proteins throughout the plant kingdom are an indication of an indispensable function in plants, but their true biological role remains obscure. Crystal and solution structures for several homologues have shown a similar overall fold with a vast internal cavity which, together with structural similarities to the steroidogenic acute regulatory protein-related lipid transfer domain and cytokinin-specific binding proteins, strongly indicate a ligand-binding role for the PR-10 proteins. This article describes the structure of a complex between a classic PR-10 protein [Lupinus luteus (yellow lupine) PR-10 protein of subclass 2, LlPR-10.2B] and N,N'-diphenylurea, a synthetic cytokinin. Synthetic cytokinins have been shown in various bioassays to exhibit activity similar to that of natural cytokinins. The present 1.95 A resolution crystallographic model reveals four N,N'-diphenylurea molecules in the hydrophobic cavity of the protein and a degree of conformational changes accompanying ligand binding. The structural adaptability of LlPR-10.2B and its ability to bind different cytokinins suggest that this protein, and perhaps other PR-10 proteins as well, can act as a reservoir of cytokinin molecules in the aqueous environment of a plant cell. Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein.,Fernandes H, Bujacz A, Bujacz G, Jelen F, Jasinski M, Kachlicki P, Otlewski J, Sikorski MM, Jaskolski M FEBS J. 2009 Mar;276(6):1596-609. Epub 2009 Feb 11. PMID:19220853 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

spinqualitylabelsall models 3e85, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image