PDBsum entry: 1dcf

Transferase

PDB id: 1dcf

Contents

Protein chain

133 a.a. *

Waters ×41

* Residue conservation analysis

PDB id:

1dcf

Name:

Transferase

Title:

Crystal structure of the receiver domain of the ethylene receptor of arabidopsis thaliana

Structure:

Etr1 protein. Chain: a. Fragment: receiver domain. Engineered: yes

Source:

Arabidopsis thaliana. Thale cress. Organism_taxid: 3702. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PDB file)

Resolution:

2.50Å R-factor: 0.222 R-free: 0.271

Authors:

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

Key ref:

H.J.Müller-Dieckmann et al. (1999). The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1. Structure, 7, 1547-1556. PubMed id: 10647185 DOI: 10.1016/S0969-2126(00)88345-8

Date:

04-Nov-99 Release date: 04-Jan-00

Protein chain

P49333  (ETR1_ARATH) -  Ethylene receptor 1

Seq: 738 a.a.

Struc: 133 a.a.*

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: E.C.2.7.13.3 - Histidine kinase.
• Reaction: ATP + protein L-histidine = ADP + protein N-phospho-L-histidine

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 Gene Ontology (GO) functional annotation 

• Biological process: two-component signal transduction system (phosphorelay) (2 terms)
• Biochemical function: two-component response regulator activity (1 term)

reference

DOI no: 10.1016/S0969-2126(00)88345-8

Structure 7:1547-1556 (1999)

PubMed id: 10647185

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

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

ABSTRACT

BACKGROUND: 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. RESULTS: The monomeric form of ETRRD resembles the known structure of the bacterial receiver domain. ETRRD forms a homodimer in solution and in the crystal, an interaction that has not been described previously. Dimerization is mediated by the C terminus, which forms an extended beta sheet with the dimer-related beta-strand core. Furthermore, the loop immediately following the active site adopts an exceptional conformation. CONCLUSIONS: The three-dimensional structure of ETRRD shows the expected conformational conservation to prokaryotic receiver proteins, such as CheY and CheB, both of which are part of the chemotaxis signaling pathway. ETRRD provides the first detailed example of a dimerized receiver domain. Given that the dimer interface of ETRRD coincides with the phosphorylation-dependent interfaces of CheY and CheB, we suggest that the monomerization of ETRRD is phosphorylation-dependent too. In the Mg(2+)-free form of ETRRD, the gamma-loop conformation does not allow a comparable interaction as observed in the active-site architectures of Mg(2+)-bound CheY from Escherichia coli and Salmonella typhimurium.

Selected figure(s)

Figure 1.
Figure 1. Ribbon representation of the ETR[RD] monomer. The order of the b strands and a helices is indicated, the position of the phosphorylatable Asp57 is shown by the red ball. The strand break at residue 78 (loop L6) is indicated by the dotted line. The figure was prepared with MOLSCRIPT [53] and RASTER3D [54].

The above figure is reprinted by permission from Cell Press: Structure (1999, 7, 1547-1556) copyright 1999.

Figure was selected by an automated process.