1DCF

CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF THE ETHYLENE RECEPTOR OF ARABIDOPSIS THALIANA

PDB DOI: https://doi.org/10.2210/pdb1DCF/pdb

Classification: TRANSFERASE
Organism(s): Arabidopsis thaliana
Expression System: Escherichia coli
Mutation(s): No

Deposited: 1999-11-04 Released: 2000-01-04
Deposition Author(s): Muller-Dieckmann, H.J., Grantz, A., Kim, S.H.

Experimental Data Snapshot

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.271
R-Value Work: 0.222
R-Value Observed: 0.227

wwPDB Validation 3D Report Full Report

This is version 1.6 of the entry. See complete history.

Literature

The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1.

Muller-Dieckmann, H.J., Grantz, A.A., Kim, S.H.

(1999) Structure 7: 1547-1556

PubMed: 10647185 Search on PubMed
DOI: https://doi.org/10.1016/s0969-2126(00)88345-8
Primary Citation of Related Structures:
1DCF

PubMed Abstract:
In Arabidopsis thaliana, ethylene perception and signal transduction into the cell are carried out by a family of membrane-bound receptors, one of which is ethylene resistant 1 (ETR1). The large cytoplasmic domain of the receptor showed significant sequence homology to the proteins of a common bacterial regulatory pathway, the two-component system. This system consists of a transmitter histidine kinase and a response regulator (or signal receiver). We present the crystal structures of the first plant receiver domain ETRRD (residues 604-738) of ETR1 in two conformations.

Organizational Affiliation

Physical Biosciences Division of Lawrence Berkeley National Laboratory, USA.

Macromolecule Content

Total Structure Weight: 15.3 kDa
Atom Count: 1,061
Modelled Residue Count: 133
Deposited Residue Count: 136
Unique protein chains: 1

Macromolecules

Find similar proteins by:

(by identity cutoff) | 3D Structure

Entity ID: 1
Molecule	Chains	Sequence Length	Organism	Details	Image
ETR1 PROTEIN	A	136	Arabidopsis thaliana	Mutation(s): 0 EC: 2.7.3
UniProt
Find proteins for P49333 (Arabidopsis thaliana) Explore P49333 Go to UniProtKB: P49333
Entity Groups
Sequence Clusters	30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt Group	P49333
Sequence Annotations Expand
Reference Sequence

Experimental Data & Validation

Experimental Data

Method: X-RAY DIFFRACTION
Resolution: 2.50 Å
R-Value Free: 0.271
R-Value Work: 0.222
R-Value Observed: 0.227
Space Group: P 4₃ 2₁ 2

Unit Cell:

Length ( Å )	Angle ( ˚ )
a = 47.92	α = 90
b = 47.92	β = 90
c = 111.79	γ = 90

Software Package:

Software Name	Purpose
SOLVE	phasing
CNS	refinement
SCALEPACK	data scaling

Structure Validation

View Full Validation Report

Entry History

Deposition Data

Released Date: 2000-01-04

Deposition Author(s):

Muller-Dieckmann, H.J.

Revision History (Full details and data files)

Version 1.0: 2000-01-04
Type: Initial release
Version 1.1: 2008-04-27
Changes: Version format compliance
Version 1.2: 2011-07-13
Changes: Version format compliance
Version 1.3: 2016-12-14
Changes: Other
Version 1.4: 2017-10-04
Changes: Refinement description
Version 1.5: 2018-01-31
Changes: Experimental preparation
Version 1.6: 2024-02-07
Changes: Data collection, Database references

RCSB PDB Core Operations are funded by the National Science Foundation (DBI-1832184), the US Department of Energy (DE-SC0019749), and the National Cancer Institute, National Institute of Allergy and Infectious Diseases, and National Institute of General Medical Sciences of the National Institutes of Health under grant R01GM133198.