2vea

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{{Seed}}
 
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[[Image:2vea.jpg|left|200px]]
 
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==The complete sensory module of the cyanobacterial phytochrome Cph1 in the Pr-state.==
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The line below this paragraph, containing "STRUCTURE_2vea", creates the "Structure Box" on the page.
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<StructureSection load='2vea' size='340' side='right'caption='[[2vea]], [[Resolution|resolution]] 2.21&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2vea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synechocystis_sp._PCC_6803 Synechocystis sp. PCC 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2VEA FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.21&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CYC:PHYCOCYANOBILIN'>CYC</scene></td></tr>
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{{STRUCTURE_2vea| PDB=2vea | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2vea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2vea OCA], [https://pdbe.org/2vea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2vea RCSB], [https://www.ebi.ac.uk/pdbsum/2vea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2vea ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PHY1_SYNY3 PHY1_SYNY3] Regulatory photoreceptor which exists in two forms that are reversibly interconvertible by light: the R form that absorbs maximally in the red region of the spectrum and the FR form that absorbs maximally in the far-red region. Has also a slight blue shift for the far-red maximum. Forms a two-component system with the rcp1 response regulator.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/2vea_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2vea ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Phytochromes are red/far-red photochromic biliprotein photoreceptors, which in plants regulate seed germination, stem extension, flowering time, and many other light effects. However, the structure/functional basis of the phytochrome photoswitch is still unclear. Here, we report the ground state structure of the complete sensory module of Cph1 phytochrome from the cyanobacterium Synechocystis 6803. Although the phycocyanobilin (PCB) chromophore is attached to Cys-259 as expected, paralleling the situation in plant phytochromes but contrasting to that in bacteriophytochromes, the ZZZssa conformation does not correspond to that expected from Raman spectroscopy. We show that the PHY domain, previously considered unique to phytochromes, is structurally a member of the GAF (cGMP phosphodiesterase/adenylyl cyclase/FhlA) family. Indeed, the tandem-GAF dumbbell revealed for phytochrome sensory modules is remarkably similar to the regulatory domains of cyclic nucleotide (cNMP) phosphodiesterases and adenylyl cyclases. A unique feature of the phytochrome structure is a long, tongue-like protrusion from the PHY domain that seals the chromophore pocket and stabilizes the photoactivated far-red-absorbing state (Pfr). The tongue carries a conserved PRxSF motif, from which an arginine finger points into the chromophore pocket close to ring D forming a salt bridge with a conserved aspartate residue. The structure that we present provides a framework for light-driven signal transmission in phytochromes.
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===THE COMPLETE SENSORY MODULE OF THE CYANOBACTERIAL PHYTOCHROME CPH1 IN THE PR-STATE.===
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The structure of a complete phytochrome sensory module in the Pr ground state.,Essen LO, Mailliet J, Hughes J Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14709-14. Epub 2008 Sep 17. PMID:18799745<ref>PMID:18799745</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_18799745}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 2vea" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 18799745 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18799745}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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2VEA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechocystis_sp._pcc_6803 Synechocystis sp. pcc 6803]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2VEA OCA].
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[[Category: Synechocystis sp. PCC 6803]]
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[[Category: Essen L-O]]
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==Reference==
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[[Category: Hughes J]]
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The structure of a complete phytochrome sensory module in the Pr ground state., Essen LO, Mailliet J, Hughes J, Proc Natl Acad Sci U S A. 2008 Sep 23;105(38):14709-14. Epub 2008 Sep 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18799745 18799745]
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[[Category: Mailliet J]]
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[[Category: Single protein]]
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[[Category: Synechocystis sp. pcc 6803]]
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[[Category: Essen, L O.]]
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[[Category: Hughes, J.]]
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[[Category: Mailliet, J.]]
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[[Category: Arginine finger]]
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[[Category: Bilin-like chromophore]]
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[[Category: Chromophore]]
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[[Category: Kinase]]
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[[Category: Knot]]
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[[Category: Pas domain]]
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[[Category: Phosphorylation]]
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[[Category: Photoreceptor]]
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[[Category: Photoreceptor protein]]
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[[Category: Phytochrome]]
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[[Category: Receptor]]
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[[Category: Sensory transduction]]
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[[Category: Tandem gaf domain]]
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[[Category: Transferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Oct 1 21:36:25 2008''
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Current revision

The complete sensory module of the cyanobacterial phytochrome Cph1 in the Pr-state.

PDB ID 2vea

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