1h6r

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{{Seed}}
 
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[[Image:1h6r.png|left|200px]]
 
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==The oxidized state of a redox sensitive variant of green fluorescent protein==
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The line below this paragraph, containing "STRUCTURE_1h6r", creates the "Structure Box" on the page.
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<StructureSection load='1h6r' size='340' side='right'caption='[[1h6r]], [[Resolution|resolution]] 1.50&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'>[[1h6r]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1H6R 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]] 1.5&#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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=PIA:[(4Z)-2-[(1S)-1-AMINOETHYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>PIA</scene></td></tr>
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{{STRUCTURE_1h6r| PDB=1h6r | 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=1h6r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h6r OCA], [https://pdbe.org/1h6r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1h6r RCSB], [https://www.ebi.ac.uk/pdbsum/1h6r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1h6r ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GFP_AEQVI GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.
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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/h6/1h6r_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1h6r 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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To visualize the formation of disulfide bonds in living cells, a pair of redox-active cysteines was introduced into the yellow fluorescent variant of green fluorescent protein. Formation of a disulfide bond between the two cysteines was fully reversible and resulted in a &gt;2-fold decrease in the intrinsic fluorescence. Inter conversion between the two redox states could thus be followed in vitro as well as in vivo by non-invasive fluorimetric measurements. The 1.5 A crystal structure of the oxidized protein revealed a disulfide bond-induced distortion of the beta-barrel, as well as a structural reorganization of residues in the immediate chromophore environment. By combining this information with spectroscopic data, we propose a detailed mechanism accounting for the observed redox state-dependent fluorescence. The redox potential of the cysteine couple was found to be within the physiological range for redox-active cysteines. In the cytoplasm of Escherichia coli, the protein was a sensitive probe for the redox changes that occur upon disruption of the thioredoxin reductive pathway.
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===THE OXIDIZED STATE OF A REDOX SENSITIVE VARIANT OF GREEN FLUORESCENT PROTEIN===
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Shedding light on disulfide bond formation: engineering a redox switch in green fluorescent protein.,Ostergaard H, Henriksen A, Hansen FG, Winther JR EMBO J. 2001 Nov 1;20(21):5853-62. PMID:11689426<ref>PMID:11689426</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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<div class="pdbe-citations 1h6r" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11689426}}, adds the Publication Abstract to the page
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*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11689426 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11689426}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1H6R is a 3 chains structure of sequences from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1H6R OCA].
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==Reference==
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<ref group="xtra">PMID:11689426</ref><references group="xtra"/>
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[[Category: Aequorea victoria]]
[[Category: Aequorea victoria]]
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[[Category: Hansen, F G.]]
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[[Category: Large Structures]]
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[[Category: Henriksen, A.]]
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[[Category: Hansen FG]]
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[[Category: Ostergaard, H.]]
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[[Category: Henriksen A]]
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[[Category: Winther, J R.]]
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[[Category: Ostergaard H]]
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[[Category: Green fluorescent protein]]
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[[Category: Winther JR]]
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[[Category: Luminescence]]
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[[Category: Luminescent protein]]
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[[Category: Yellow-emission]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jun 25 11:30:07 2009''
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Current revision

The oxidized state of a redox sensitive variant of green fluorescent protein

PDB ID 1h6r

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