6gel

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Current revision (05:15, 21 November 2024) (edit) (undo)
 
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<StructureSection load='6gel' size='340' side='right'caption='[[6gel]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
<StructureSection load='6gel' size='340' side='right'caption='[[6gel]], [[Resolution|resolution]] 2.51&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6gel]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GEL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6GEL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6gel]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria] and [https://en.wikipedia.org/wiki/Opsanus_tau Opsanus tau]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GEL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GEL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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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]] 2.51&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</scene>, <scene name='pdbligand=CRF:[(4Z)-2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CRF</scene></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=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</scene>, <scene name='pdbligand=CRF:[(4Z)-2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(1H-INDOL-3-YLMETHYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL]ACETIC+ACID'>CRF</scene>, <scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PG4:TETRAETHYLENE+GLYCOL'>PG4</scene></td></tr>
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<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=6gel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gel OCA], [http://pdbe.org/6gel PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6gel RCSB], [http://www.ebi.ac.uk/pdbsum/6gel PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6gel ProSAT]</span></td></tr>
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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=6gel FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gel OCA], [https://pdbe.org/6gel PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gel RCSB], [https://www.ebi.ac.uk/pdbsum/6gel PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gel ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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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[https://www.uniprot.org/uniprot/W5IDB2_OPSTA W5IDB2_OPSTA] [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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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The quality of genetically encoded calcium indicators (GECIs) has improved dramatically in recent years, but high-performing ratiometric indicators are still rare. Here we describe a series of fluorescence resonance energy transfer (FRET)-based calcium biosensors with a reduced number of calcium binding sites per sensor. These 'Twitch' sensors are based on the C-terminal domain of Opsanus troponin C. Their FRET responses were optimized by a large-scale functional screen in bacterial colonies, refined by a secondary screen in rat hippocampal neuron cultures. We tested the in vivo performance of the most sensitive variants in the brain and lymph nodes of mice. The sensitivity of the Twitch sensors matched that of synthetic calcium dyes and allowed visualization of tonic action potential firing in neurons and high resolution functional tracking of T lymphocytes. Given their ratiometric readout, their brightness, large dynamic range and linear response properties, Twitch sensors represent versatile tools for neuroscience and immunology.
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Forster resonance energy transfer (FRET) between mutants of green fluorescent protein is widely used to monitor protein-protein interactions and as a readout mode in fluorescent biosensors. Despite the fundamental importance of distance and molecular angles of fluorophores to each other, structural details on fluorescent protein FRET have been missing. Here, we report the high-resolution x-ray structure of the fluorescent proteins mCerulean3 and cpVenus within the biosensor Twitch-2B, as they undergo FRET and characterize the dynamics of this biosensor with B02 -dependent paramagnetic nuclear magnetic resonance at 900 MHz and 1.1 GHz. These structural data provide the unprecedented opportunity to calculate FRET from the x-ray structure and to compare it to experimental data in solution. We find that interdomain dynamics limits the FRET effect and show that a rigidification of the sensor further enhances FRET.
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Optimized ratiometric calcium sensors for functional in vivo imaging of neurons and T lymphocytes.,Thestrup T, Litzlbauer J, Bartholomaus I, Mues M, Russo L, Dana H, Kovalchuk Y, Liang Y, Kalamakis G, Laukat Y, Becker S, Witte G, Geiger A, Allen T, Rome LC, Chen TW, Kim DS, Garaschuk O, Griesinger C, Griesbeck O Nat Methods. 2014 Feb;11(2):175-82. doi: 10.1038/nmeth.2773. Epub 2014 Jan 5. PMID:24390440<ref>PMID:24390440</ref>
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Dynamic tuning of FRET in a green fluorescent protein biosensor.,Trigo-Mourino P, Thestrup T, Griesbeck O, Griesinger C, Becker S Sci Adv. 2019 Aug 7;5(8):eaaw4988. doi: 10.1126/sciadv.aaw4988. eCollection 2019 , Aug. PMID:31457088<ref>PMID:31457088</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
<div class="pdbe-citations 6gel" style="background-color:#fffaf0;"></div>
<div class="pdbe-citations 6gel" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aequorea victoria]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Becker, S]]
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[[Category: Opsanus tau]]
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[[Category: Griesbeck, O]]
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[[Category: Becker S]]
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[[Category: Griesinger, C]]
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[[Category: Griesbeck O]]
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[[Category: Mourino, P Trigo]]
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[[Category: Griesinger C]]
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[[Category: Paulat, M]]
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[[Category: Paulat M]]
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[[Category: Thestrup, T]]
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[[Category: Thestrup T]]
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[[Category: Fluorescent protein]]
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[[Category: Trigo Mourino P]]
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[[Category: Fret]]
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[[Category: Ratiometric biosensor]]
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[[Category: Twitch-2b]]
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Current revision

The structure of TWITCH-2B

PDB ID 6gel

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