2aha

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{{Seed}}
 
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[[Image:2aha.png|left|200px]]
 
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==Crystal structure analysis of a rate-enhanced variant of redox-sensitive green fluorescent protein in the reduced form, roGFP1-R8.==
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The line below this paragraph, containing "STRUCTURE_2aha", creates the "Structure Box" on the page.
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<StructureSection load='2aha' size='340' side='right'caption='[[2aha]], [[Resolution|resolution]] 1.98&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'>[[2aha]] is a 2 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=2AHA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHA 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]] 1.98&#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=GYS:[(4Z)-2-(1-AMINO-2-HYDROXYETHYL)-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>GYS</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_2aha| PDB=2aha | 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=2aha FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2aha OCA], [https://pdbe.org/2aha PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2aha RCSB], [https://www.ebi.ac.uk/pdbsum/2aha PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2aha 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/ah/2aha_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=2aha 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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Redox-sensitive variants of the green fluorescent protein (roGFPs) had previously been developed that allow "real-time" monitoring of the redox status of cellular compartments by fluorescence excitation ratiometry. However, the response time of these probes limits the study of certain rapid oxidative events, such as H2O2 bursts in cell signaling. The substitution of up to three positively charged amino acids adjacent to the introduced disulfide in roGFP1 (variants designated roGFP1-R1 through -R14) substantially improved the response rate. The pseudo first-order rate constants for oxidation by H2O2 and reduction by DTT and redox midpoint potentials were determined. The rate constants approximately doubled with each additional positively charged substitution, to nearly an order of magnitude total. The midpoint potentials are highly correlated with the rate increases, becoming more oxidizing with increasing numbers of positive substitutions. Crystal structures of two variants with opposite disulfide oxidation states have been determined: a 2.2 A resolution structure of oxidized "R7" containing two basic substitutions, and a 1.95 A resolution structure of reduced "R8" with one basic and one acidic substitution. Nonlinear Poisson-Boltzmann (PB) calculations are shown to accurately predict the effects of the substitutions on the rate constants. The effects of the substitutions on dimer formation, relative oxidative midpoint potentials, and oxidation and reduction rates are discussed. roGFPs are demonstrated to constitute an excellent model system for quantitative analysis of factors influencing thiol transfer reactions. roGFP1-R12 is most suitable for use in live cells, due to significantly increased reaction rate and increased pI.
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===Crystal structure analysis of a rate-enhanced variant of redox-sensitive green fluorescent protein in the reduced form, roGFP1-R8.===
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Re-engineering redox-sensitive green fluorescent protein for improved response rate.,Cannon MB, Remington SJ Protein Sci. 2006 Jan;15(1):45-57. Epub 2005 Dec 1. PMID:16322566<ref>PMID:16322566</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 2aha" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16322566}}, 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 16322566 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16322566}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2AHA is a 2 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=2AHA OCA].
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==Reference==
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<ref group="xtra">PMID:16322566</ref><references group="xtra"/>
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[[Category: Aequorea victoria]]
[[Category: Aequorea victoria]]
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[[Category: Cannon, M B.]]
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[[Category: Large Structures]]
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[[Category: Remington, S J.]]
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[[Category: Cannon MB]]
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[[Category: Beta barrel]]
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[[Category: Remington SJ]]
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[[Category: Chromophore]]
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[[Category: Disulfide]]
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[[Category: Luminescent protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat Jul 4 18:14:54 2009''
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Current revision

Crystal structure analysis of a rate-enhanced variant of redox-sensitive green fluorescent protein in the reduced form, roGFP1-R8.

PDB ID 2aha

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