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- SASDCA7: Ethylene Receptor 1 (DHp + CA domains) (Ethylene receptor 1 dimer... -

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Basic information

Entry
Database: SASBDB / ID: SASDCA7
SampleEthylene Receptor 1 (DHp + CA domains)
  • Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains (protein), ETR1_DHp-CA, Arabidopsis thaliana
Function / homology
Function and homology information


ethylene receptor activity / regulation of seedling development / detection of ethylene stimulus / ethylene binding / seed dormancy process / defense response by callose deposition in cell wall / negative regulation of ethylene-activated signaling pathway / sugar mediated signaling pathway / response to gibberellin / phloem or xylem histogenesis ...ethylene receptor activity / regulation of seedling development / detection of ethylene stimulus / ethylene binding / seed dormancy process / defense response by callose deposition in cell wall / negative regulation of ethylene-activated signaling pathway / sugar mediated signaling pathway / response to gibberellin / phloem or xylem histogenesis / response to insect / response to ethylene / cytokinin metabolic process / response to auxin / regulation of stomatal movement / protein histidine kinase activity / response to abscisic acid / hydrogen peroxide biosynthetic process / histidine kinase / phosphorelay sensor kinase activity / response to salt stress / response to molecule of bacterial origin / defense response / response to heat / defense response to bacterium / cell division / endoplasmic reticulum membrane / endoplasmic reticulum / ATP binding / identical protein binding / metal ion binding
Similarity search - Function
Ethylene receptor / His Kinase A (phospho-acceptor) domain / His Kinase A (phosphoacceptor) domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain / Signal transduction histidine kinase-related protein, C-terminal / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / Histidine kinase domain / Histidine kinase domain profile. / Response regulator receiver domain / cheY-homologous receiver domain ...Ethylene receptor / His Kinase A (phospho-acceptor) domain / His Kinase A (phosphoacceptor) domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain / Signal transduction histidine kinase-related protein, C-terminal / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / Histidine kinase domain / Histidine kinase domain profile. / Response regulator receiver domain / cheY-homologous receiver domain / Signal transduction response regulator, receiver domain / Response regulatory domain profile. / CheY-like superfamily / GAF domain / Domain present in phytochromes and cGMP-specific phosphodiesterases. / GAF domain / GAF-like domain superfamily / Histidine kinase-, DNA gyrase B-, and HSP90-like ATPase / Histidine kinase-like ATPases / Histidine kinase/HSP90-like ATPase / Histidine kinase/HSP90-like ATPase superfamily
Similarity search - Domain/homology
Biological speciesArabidopsis thaliana (thale cress)
CitationJournal: J Biol Chem / Year: 2015
Title: Structural model of the cytosolic domain of the plant ethylene receptor 1 (ETR1).
Authors: Hubert Mayerhofer / Saravanan Panneerselvam / Heidi Kaljunen / Anne Tuukkanen / Haydyn D T Mertens / Jochen Mueller-Dieckmann /
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 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.
Contact author
  • Haydyn Mertens (EMBL-Hamburg, European Molecular Biology Laboratory (EMBL) - Hamburg outstation, Notkestraße 85, Geb. 25A, 22607 Hamburg, Deutschland, Germany)

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Structure visualization

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Models

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Sample

SampleName: Ethylene Receptor 1 (DHp + CA domains) / Dry vol: 33262 / Specimen concentration: 0.60-6.00 / Concentration method: A280
BufferName: 20 mM Tris 150 mM NaCl 1 mM DTT 5 mM ADP / pH: 8.8
Entity #778Name: ETR1_DHp-CA / Type: protein
Description: Ethylene receptor 1 dimerization histidine phosphotransfer + catalytic ATP-binding domains
Formula weight: 27.492 / Num. of mol.: 2 / Source: Arabidopsis thaliana / References: UniProt: P49333
Sequence: TAIRARNDFL AVMNHEMRTP MHAIIALSSL LQETELTPEQ RLMVETILKS SNLLATLMND VLDLSRLEDG SLQLELGTFN LHTLFREVLN LIKPIAVVKK LPITLNLAPD LPEFVVGDEK RLMQIILNIV GNAVKFSKQG SISVTALVTK SDTRAADFFV VPTGSHFYLR ...Sequence:
TAIRARNDFL AVMNHEMRTP MHAIIALSSL LQETELTPEQ RLMVETILKS SNLLATLMND VLDLSRLEDG SLQLELGTFN LHTLFREVLN LIKPIAVVKK LPITLNLAPD LPEFVVGDEK RLMQIILNIV GNAVKFSKQG SISVTALVTK SDTRAADFFV VPTGSHFYLR VKVKDSGAGI NPQDIPKIFT KFAQTQSLAT RSSGGSGLGL AISKRFVNLM EGNIWIESDG LGKGCTAIFD VKLGISERSN E

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Experimental information

BeamInstrument name: DORIS III X33 / City: Hamburg / : Germany / Shape: 0.6 / Type of source: X-ray synchrotron / Wavelength: 0.154 Å / Dist. spec. to detc.: 3.1 mm
DetectorName: Pilatus 1M-W / Pixsize x: 0.172 mm
Scan
Title: ETR1_DHp-CA / Measurement date: Oct 11, 2010 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 15 sec. / Number of frames: 8 / Unit: 1/nm /
MinMax
Q0.1903 6.0155
Distance distribution function P(R)
Sofotware P(R): GNOM 4.6 / Number of points: 476 /
MinMax
Q0.1916 2.79
P(R) point49 524
R0 8
Result
Type of curve: extrapolated
ExperimentalExperimental errorStandardStandard errorPorodPorod error
MW46 kDa5 24.9 kDa2 46 kDa5
Volume----73.6 nm35

P(R)P(R) errorGuinierGuinier error
Forward scattering, I019.8 0.1 19.84 1
Radius of gyration, Rg2.76 nm0.1 2.72 nm0.2

MinMaxError
D-8.7 0.5
Guinier point1 106 -

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