4pl9

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Structure of the catalytic domain of ETR1 from Arabidopsis thalianaStructure of the catalytic domain of ETR1 from Arabidopsis thaliana

Structural highlights

4pl9 is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.9Å
Ligands:, , ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ETR1_ARATH Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.[1] [2]

Publication Abstract from PubMed

Ethylene initiates important aspects of plant growth and development through disulfide- linked receptor dimers, located in the endoplasmic reticulum. The receptors feature a small trans-membrane, 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 signalling pathway. Here we report the crystallographic structures of the ETR1 Catalytic ATP-binding (CA) and the Ethylene response sensor 1 (ERS1) Dimerization Histidine phosphotransfer (DHp) domains and the solution structure of the entire cytosolic domain of ETR1, all from A. thaliana. The isolated dimeric ERS1 DHp domain is asymmetric, the result of different helical bending angles close to the conserved His residue. The structures of the CA, DHp and receiver domains of ethylene receptors and of a homologous, but dissimilar, GAF domain were refined against experimental SAXS 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 different position 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-signalling pathway. Our model, therefore, provides the first step towards a detailed understanding of the molecular mechanics of this important signal transduction process in plants.

Structural Model of the Cytosolic Domain of the Plant Ethylene Receptor 1 (ETR1).,Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J J Biol Chem. 2014 Dec 1. pii: jbc.M114.587667. PMID:25451923[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Qu X, Schaller GE. Requirement of the histidine kinase domain for signal transduction by the ethylene receptor ETR1. Plant Physiol. 2004 Oct;136(2):2961-70. Epub 2004 Oct 1. PMID:15466228 doi:http://dx.doi.org/10.1104/pp.104.047126
  2. O'Malley RC, Rodriguez FI, Esch JJ, Binder BM, O'Donnell P, Klee HJ, Bleecker AB. Ethylene-binding activity, gene expression levels, and receptor system output for ethylene receptor family members from Arabidopsis and tomato. Plant J. 2005 Mar;41(5):651-9. PMID:15703053 doi:http://dx.doi.org/10.1111/j.1365-313X.2004.02331.x
  3. Mayerhofer H, Panneerselvam S, Kaljunen H, Tuukkanen A, Mertens HD, Mueller-Dieckmann J. Structural Model of the Cytosolic Domain of the Plant Ethylene Receptor 1 (ETR1). J Biol Chem. 2014 Dec 1. pii: jbc.M114.587667. PMID:25451923 doi:http://dx.doi.org/10.1074/jbc.M114.587667

4pl9, resolution 1.90Å

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