3E85

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

Summary for 3E85

• Entry DOI: 10.2210/pdb3e85/pdb
• Related: 1BV1 1ICX 1IFV 1XDF 2FLH 2QIM
• Descriptor: PR10.2B, 1,3-DIPHENYLUREA, SODIUM ION, ... (4 entities in total)
• Functional Keywords: plant hormones, cytokinin, diphenylurea, plant pr-10 protein, yellow lupine, pathogenesis-related protein, plant defense, plant protein
• Biological source: Lupinus luteus (European yellow lupin)
• Total number of polymer chains: 1
• Total formula weight: 17800.97

Authors

Fernandes, H.C.,Bujacz, G.,Bujacz, A.,Sikorski, M.M.,Jaskolski, M. (deposition date: 2008-08-19, release date: 2009-03-03, Last modification date: 2023-08-30)

Primary citation

Fernandes, H.,Bujacz, A.,Bujacz, G.,Jelen, F.,Jasinski, M.,Kachlicki, P.,Otlewski, J.,Sikorski, M.M.,Jaskolski, M.
Cytokinin-induced structural adaptability of a Lupinus luteus PR-10 protein.
Febs J., 276:1596-1609, 2009

PubMed Abstract: 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.

PubMed: 19220853
DOI: 10.1111/j.1742-4658.2009.06892.x

Experimental method

X-RAY DIFFRACTION (1.95 Å)