4PL9

Structure of the catalytic domain of ETR1 from Arabidopsis thaliana

Summary for 4PL9

• Entry DOI: 10.2210/pdb4pl9/pdb
• Descriptor: Ethylene receptor 1, CADMIUM ION, CHLORIDE ION, ... (6 entities in total)
• Functional Keywords: etr1, histidine kinase, ethylene receptor, cadmium, adp, transferase
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Endoplasmic reticulum membrane ; Multi-pass membrane protein : P49333
• Total number of polymer chains: 1
• Total formula weight: 21570.14

Authors

Panneerselvam, S.,Mueller-Dieckmann, J. (deposition date: 2014-05-16, release date: 2014-12-17, Last modification date: 2024-05-08)

Primary citation

Mayerhofer, H.,Panneerselvam, S.,Kaljunen, H.,Tuukkanen, A.,Mertens, H.D.,Mueller-Dieckmann, J.
Structural Model of the Cytosolic Domain of the Plant Ethylene Receptor 1 (ETR1).
J.Biol.Chem., 290:2644-2658, 2015

PubMed Abstract: Ethylene initiates important aspects of plant growth and development through disulfide-linked receptor dimers located in the endoplasmic reticulum. The receptors feature a small transmembrane, ethylene binding domain followed by a large cytosolic domain, which serves as a scaffold for the assembly of large molecular weight complexes of different ethylene receptors and other cellular participants of the ethylene signaling pathway. Here we report the crystallographic structures of the ethylene receptor 1 (ETR1) catalytic ATP-binding and the ethylene response sensor 1 dimerization histidine phosphotransfer (DHp) domains and the solution structure of the entire cytosolic domain of ETR1, all from Arabidopsis thaliana. The isolated dimeric ethylene response sensor 1 DHp domain is asymmetric, the result of different helical bending angles close to the conserved His residue. The structures of the catalytic ATP-binding, DHp, and receiver domains of ethylene receptors and of a homologous, but dissimilar, GAF domain were refined against experimental small angle x-ray scattering data, leading to a structural model of the entire cytosolic domain of the ethylene receptor 1. The model illustrates that the cytosolic domain is shaped like a dumbbell and that the receiver domain is flexible and assumes a position different from those observed in prokaryotic histidine kinases. Furthermore the cytosolic domain of ETR1 plays a key role, interacting with all other receptors and several participants of the ethylene signaling pathway. Our model, therefore, provides the first step toward a detailed understanding of the molecular mechanics of this important signal transduction process in plants.

PubMed: 25451923
DOI: 10.1074/jbc.M114.587667

Experimental method

X-RAY DIFFRACTION (1.9 Å)