2QIM

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

Summary for 2QIM

• Entry DOI: 10.2210/pdb2qim/pdb
• Related: 1BV1 1E09 1FM4 1ICX 1IFV 1XDF 2FLH
• Descriptor: PR10.2B, CALCIUM ION, (2E)-2-methyl-4-(9H-purin-6-ylamino)but-2-en-1-ol, ... (5 entities in total)
• Functional Keywords: trans-zeatin, cytokinin, plant hormones, plant protein, pr-10 protein, pathogenesis-related protein, allergen
• Biological source: Lupinus luteus (yellow lupine)
• Total number of polymer chains: 1
• Total formula weight: 17915.14

Authors

Fernandes, H.C.,Pasternak, O.,Bujacz, G.,Bujacz, A.,Sikorski, M.M.,Jaskolski, M. (deposition date: 2007-07-05, release date: 2008-04-29, Last modification date: 2024-04-03)

Primary citation

Fernandes, H.,Pasternak, O.,Bujacz, G.,Bujacz, A.,Sikorski, M.M.,Jaskolski, M.
Lupinus luteus pathogenesis-related protein as a reservoir for cytokinin.
J.Mol.Biol., 378:1040-1051, 2008

PubMed Abstract: Plant pathogenesis-related (PR) proteins of class 10 (PR-10) are small and cytosolic. The main feature of their three-dimensional structure is a large cavity between a seven-stranded antiparallel beta-sheet and a long C-terminal alpha-helix. Although PR-10 proteins are abundant in plants, their physiological role remains unknown. Recent data have indicated ligand binding as their possible biological function. The article describes the structure of a complex between a classic PR-10 protein (yellow lupine LlPR-10.2B) and the plant hormone, trans-zeatin. Previously, trans-zeatin binding has been reported in a structurally related cytokinin-specific binding protein, which has a distant sequence relation with classic PR-10 proteins. In the present 1.35 A resolution crystallographic model, three perfectly ordered zeatin molecules are found in the binding cavity of the protein. The fact that three zeatin molecules are bound by the protein when only a fourfold molar excess of the ligand was used indicates an unusual type of affinity for this ligand and suggests that LlPR-10.2B, and perhaps other PR-10 proteins as well, acts as a reservoir of cytokinin molecules in the aqueous environment of the cell.

PubMed: 18406424
DOI: 10.1016/j.jmb.2008.03.027

Experimental method

X-RAY DIFFRACTION (1.35 Å)