|
|
| Line 3: |
Line 3: |
| | <StructureSection load='3ed8' size='340' side='right'caption='[[3ed8]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3ed8' size='340' side='right'caption='[[3ed8]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3ed8]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ED8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3ED8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3ed8]] is a 5 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=3ED8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ED8 FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CRO:{2-[(1R,2R)-1-AMINO-2-HYDROXYPROPYL]-4-(4-HYDROXYBENZYLIDENE)-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CRO</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=3ed8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ed8 OCA], [http://pdbe.org/3ed8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ed8 RCSB], [http://www.ebi.ac.uk/pdbsum/3ed8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ed8 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=3ed8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ed8 OCA], [https://pdbe.org/3ed8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ed8 RCSB], [https://www.ebi.ac.uk/pdbsum/3ed8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ed8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [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. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 33: |
Line 35: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Aeqvi]] | + | [[Category: Aequorea victoria]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ottmann, C]] | + | [[Category: Ottmann C]] |
| - | [[Category: Weyand, M]] | + | [[Category: Weyand M]] |
| - | [[Category: Bimolecular fluorescence complementation]]
| + | |
| - | [[Category: Luminescent protein]]
| + | |
| - | [[Category: Superfolder]]
| + | |
| Structural highlights
Function
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.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Abstract Bimolecular fluorescence complementation (BiFC) using yellow fluorescent protein (YFP) is a widely employed method to study protein-protein interactions in cells. As yet, this technique has not been used in vitro. To evaluate a possible application of BiFC in vitro, we constructed a 'superfolder split YFP' system where 15 mutations enhance expression of the fusion proteins in Escherichia coli and enable a native purification due to improved solubility. Here, we present the crystal structure of 'superfolder YFP', providing the structural basis for the enhanced folding and stability characteristics. Complementation between the two non-fluorescent YFP fragments fused to HRas and Raf1RBD or to 14-3-3 and PMA2-CT52 resulted in the constitution of the functional fluorophore. The in vivo BiFC with these protein interaction pairs was demonstrated in eukaryotic cell lines as well. Here, we present for the first time BiFC in vitro studies with natively purified superfolder YFP fusion proteins and show the potential and drawbacks of this method for analyzing protein-protein interactions.
Applicability of superfolder YFP bimolecular fluorescence complementation in vitro.,Ottmann C, Weyand M, Wolf A, Kuhlmann J, Ottmann C Biol Chem. 2009 Jan;390(1):81-90. PMID:19007309[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ottmann C, Weyand M, Wolf A, Kuhlmann J, Ottmann C. Applicability of superfolder YFP bimolecular fluorescence complementation in vitro. Biol Chem. 2009 Jan;390(1):81-90. PMID:19007309 doi:10.1515/BC.2009.008
|
