4euk: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4euk]] is a 2 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=4EUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EUK FirstGlance]. <br>
<table><tr><td colspan='2'>[[4euk]] is a 2 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=4EUK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EUK FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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]] 1.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=4euk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4euk OCA], [https://pdbe.org/4euk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4euk RCSB], [https://www.ebi.ac.uk/pdbsum/4euk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4euk ProSAT]</span></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=4euk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4euk OCA], [https://pdbe.org/4euk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4euk RCSB], [https://www.ebi.ac.uk/pdbsum/4euk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4euk ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/AHK5_ARATH AHK5_ARATH] Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Negative regulator of the ETR1-dependent abscisic acid (ABA) and ethylene signaling pathway that inhibits the root elongation. Promotes stomatal closure. Regulates stomatal opening by integrating multiple signals via hydrogen peroxide H(2)O(2) homeostasis in guard cells in an ABA-independent manner. May contribute to basal defense mechanisms by closing stomata in the presence of bacterial pathogens. Regulates both hormone levels and ROS production in response to stress. Required for full immunity to bacterial pathogen and necrotrophic fungus.<ref>PMID:17202180</ref> <ref>PMID:18077346</ref> <ref>PMID:18560512</ref> <ref>PMID:22256998</ref> <ref>PMID:22827948</ref>  
[https://www.uniprot.org/uniprot/AHK5_ARATH AHK5_ARATH] Functions as a histidine kinase and transmits the stress signal to a downstream MAPK cascade. This protein undergoes an ATP-dependent autophosphorylation at a conserved histidine residue in the kinase core, and a phosphoryl group is then transferred to a conserved aspartate residue in the receiver domain. Negative regulator of the ETR1-dependent abscisic acid (ABA) and ethylene signaling pathway that inhibits the root elongation. Promotes stomatal closure. Regulates stomatal opening by integrating multiple signals via hydrogen peroxide H(2)O(2) homeostasis in guard cells in an ABA-independent manner. May contribute to basal defense mechanisms by closing stomata in the presence of bacterial pathogens. Regulates both hormone levels and ROS production in response to stress. Required for full immunity to bacterial pathogen and necrotrophic fungus.<ref>PMID:17202180</ref> <ref>PMID:18077346</ref> <ref>PMID:18560512</ref> <ref>PMID:22256998</ref> <ref>PMID:22827948</ref>  
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== Publication Abstract from PubMed ==
The multi-step phosphorelay (MSP) system defines a key signal transduction pathway in plants and many eukaryotes. In this system, external stimuli first lead to the activation of a histidine kinase, followed by transfer of a phosphoryl group from the receiver domain of the kinase (HK(RD)) to downstream, cytosolic phosphotransfer proteins (HPs). In order to establish the determinants of specificity for this signaling relay system, we have solved the first crystal structure of a plant HK(RD), AHK5(RD), in complex with one of its cognate HPs, AHP1. AHP1 binds AHK5(RD) via a prominent hydrogen bond docking ridge and a hydrophobic patch. These features are conserved among all AHP proteins, but differ significantly from other structurally characterized prokaryotic and eukaryotic HPs. Surface plasmon resonance experiments show that AHK5(RD) binds to AHP1-3 with similar, micromolar affinity, consistent with the transient nature of this signaling complex. Our correlation of structural and functional data provide the first insight, at the atomic level as well as with quantitative affinity data, into the molecular recognition events governing the MSP in plants.
Structure-Function Analysis of Arabidopsis thaliana Histidine Kinase AHK5 Bound to Its Cognate Phosphotransfer Protein AHP1.,Bauer J, Reiss K, Veerabagu M, Heunemann M, Harter K, Stehle T Mol Plant. 2013 Jan 24. PMID:23132142<ref>PMID:23132142</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 4euk" style="background-color:#fffaf0;"></div>
== References ==
== References ==
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