SASDC42: Ethylene Receptor 1 Cytosolic Domain (Ethylene Receptor 1, ETR1(-ΔTM))

Basic information

Entry

Database: SASBDB / ID: SASDC42

Sample

Ethylene Receptor 1 Cytosolic Domain

• Ethylene Receptor 1Ethylene as a plant hormone (protein), ETR1(-ΔTM), Arabidopsis thaliana

Function / homology

Function:

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 / response to insect / phloem or xylem histogenesis / response to ethylene / cytokinin metabolic process / regulation of stomatal movement / response to auxin / 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

Domain/homology:

Ethylene receptor / His Kinase A (phospho-acceptor) domain / His Kinase A (phosphoacceptor) domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain / Signal transduction histidine kinase, dimerisation/phosphoacceptor domain superfamily / Signal transduction histidine kinase-related protein, C-terminal / 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. / GAF domain / CheY-like superfamily / 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

Component:

Ethylene receptor 1

• Biological species: Arabidopsis thaliana (thale cress)
• Citation: Journal: 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 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

• Anne Tuukkanen
• Haydyn Mertens

Models

Sample

• Sample: Name: Ethylene Receptor 1 Cytosolic Domain / Dry vol: 78367 / Specimen concentration: 0.70-4.20 / Concentration method: A280
• Buffer: Name: 20 mM TRIS 150 mM NaCl 1mM DTT 250mM NDSB / Concentration: 20.00 mM / pH: 8.8 / Composition: 150 mM NaCl, 1mM DTT, 250mM NDSB

Entity #515

Name: ETR1(-ΔTM) / Type: protein / Description: Ethylene Receptor 1Ethylene as a plant hormone / Formula weight: 64.555 / Num. of mol.: 2 / Source: Arabidopsis thaliana / References: UniProt: P49333
Sequence:

DRHTILKTTL VELGRTLALE ECALWMPTRT GLELQLSYTL RHQHPVEYTV PIQLPVINQV FGTSRAVKIS PNSPVARLRP VSGKYMLGEV VAVRVPLLHL SNFQINDWPE LSTKRYALMV LMLPSDSARQ WHVHELELVE VVADQVAVAL SHAAILEESM RARDLLMEQN VALDLARREA ETAIRARNDF LAVMNHEMRT PMHAIIALSS LLQETELTPE QRLMVETILK SSNLLATLMN DVLDLSRLED GSLQLELGTF NLHTLFREVL NLIKPIAVVK KLPITLNLAP DLPEFVVGDE KRLMQIILNI VGNAVKFSKQ GSISVTALVT KSDTRAADFF VVPTGSHFYL RVKVKDSGAG INPQDIPKIF TKFAQTQSLA TRSSGGSGLG LAISKRFVNL MEGNIWIESD GLGKGCTAIF DVKLGISERS NESKQSGIPK VPAIPRHSNF TGLKVLVMDE NGVSRMVTKG LLVHLGCEVT TVSSNEECLR VVSHEHKVVF MDVCMPGVEN YQIALRIHEK FTKQRHQRPL LVALSGNTDK STKEKCMSFG LDGVLLKPVS LDNIRDVLSD LLEPRVLYEG M

Experimental information

• Beam: Instrument name: PETRA III P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 1.24 Å / Dist. spec. to detc.: 3.1 mm
• Detector: Name: Pilatus 2M

Scan

Title: ETR1-delTM / Measurement date: Mar 29, 2013 / Storage temperature: 10 °C / Cell temperature: 10 °C / Exposure time: 0.05 sec. / Number of frames: 20 / Unit: 1/nm /

	Min	Max
Q	0.0758	4.6653

Distance distribution function P(R)

Sofotware P(R): GNOM 5.0 / Number of points: 482 /

	Min	Max
Q	0.123649	1.40266
P(R) point	1	482
R	0	19

Result

Type of curve: merged / Standard: BSA / Comments: ETR1 in the absence of NDSB

	Experimental	Experimental error	Standard	Standard error	Porod	Porod error
MW	53 kDa	5	53 kDa	5	161.2 kDa	24
Volume	-	-	-	-	274 nm3	42

	P(R)	P(R) error	Guinier	Guinier error
Forward scattering, I0	1164	40	1124	25
Radius of gyration, Rg	5.9 nm	0.6	5.5 nm	1.1

	Min	Max	Error
D	-	19	0.5
Guinier point	19	42	-