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==CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF THE ETHYLENE RECEPTOR OF ARABIDOPSIS THALIANA==
==CRYSTAL STRUCTURE OF THE RECEIVER DOMAIN OF THE ETHYLENE RECEPTOR OF ARABIDOPSIS THALIANA==
<StructureSection load='1dcf' size='340' side='right' caption='[[1dcf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
<StructureSection load='1dcf' size='340' side='right'caption='[[1dcf]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1dcf]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DCF FirstGlance]. <br>
<table><tr><td colspan='2'>[[1dcf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DCF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DCF FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcf OCA], [http://pdbe.org/1dcf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1dcf RCSB], [http://www.ebi.ac.uk/pdbsum/1dcf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcf ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dcf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dcf OCA], [https://pdbe.org/1dcf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dcf RCSB], [https://www.ebi.ac.uk/pdbsum/1dcf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dcf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/ETR1_ARATH ETR1_ARATH]] Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.<ref>PMID:15466228</ref> <ref>PMID:15703053</ref>
[https://www.uniprot.org/uniprot/ETR1_ARATH ETR1_ARATH] Ethylene receptor related to bacterial two-component regulators. Acts as a redundant negative regulator of ethylene signaling.<ref>PMID:15466228</ref> <ref>PMID:15703053</ref>  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dcf_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dc/1dcf_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 18: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dcf ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dcf ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.
The structure of the signal receiver domain of the Arabidopsis thaliana ethylene receptor ETR1.,Muller-Dieckmann HJ, Grantz AA, Kim SH Structure. 1999 Dec 15;7(12):1547-56. PMID:10647185<ref>PMID:10647185</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1dcf" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Grantz, A]]
[[Category: Arabidopsis thaliana]]
[[Category: Kim, S H]]
[[Category: Large Structures]]
[[Category: Muller-Dieckmann, H J]]
[[Category: Grantz A]]
[[Category: Beta-alpha five sandwich]]
[[Category: Kim SH]]
[[Category: Transferase]]
[[Category: Muller-Dieckmann HJ]]

Latest revision as of 09:52, 7 February 2024

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

Structural highlights

1dcf 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 2.5Å
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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

1dcf, resolution 2.50Å

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