3evp: Difference between revisions
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<StructureSection load='3evp' size='340' side='right'caption='[[3evp]], [[Resolution|resolution]] 1.45Å' scene=''> | <StructureSection load='3evp' size='340' side='right'caption='[[3evp]], [[Resolution|resolution]] 1.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3evp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3evp]] is a 1 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=3EVP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3EVP FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.453Å</td></tr> | ||
<tr id=' | <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'>[https://proteopedia.org/fgij/fg.htm?mol=3evp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evp OCA], [https://pdbe.org/3evp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3evp RCSB], [https://www.ebi.ac.uk/pdbsum/3evp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3evp 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=3evp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3evp OCA], [https://pdbe.org/3evp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3evp RCSB], [https://www.ebi.ac.uk/pdbsum/3evp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3evp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == 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. | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Aequorea victoria]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Kotlikoff | [[Category: Kotlikoff MI]] | ||
[[Category: Shui | [[Category: Shui B]] | ||
[[Category: Sondermann | [[Category: Sondermann H]] | ||
[[Category: Wang | [[Category: Wang Q]] | ||
Latest revision as of 21:58, 29 November 2023
crystal structure of circular-permutated EGFPcrystal structure of circular-permutated EGFP
Structural highlights
FunctionGFP_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. Publication Abstract from PubMedGenetically encoded Ca(2+) indicators are important tools that enable the measurement of Ca(2+) dynamics in a physiologically relevant context. GCaMP2, one of the most robust indicators, is a circularly permutated EGFP (cpEGFP)/M13/calmodulin (CaM) fusion protein that has been successfully used for studying Ca(2+) fluxes in vivo in the heart and vasculature of transgenic mice. Here we describe crystal structures of bright and dim states of GCaMP2 that reveal a sophisticated molecular mechanism for Ca(2+) sensing. In the bright state, CaM stabilizes the fluorophore in an ionized state similar to that observed in EGFP. Mutational analysis confirmed critical interactions between the fluorophore and elements of the fused peptides. Solution scattering studies indicate that the Ca(2+)-free form of GCaMP2 is a compact, predocked state, suggesting a molecular basis for the relatively rapid signaling kinetics reported for this indicator. These studies provide a structural basis for the rational design of improved Ca(2+)-sensitive probes. Structural Basis for Calcium Sensing by GCaMP2.,Wang Q, Shui B, Kotlikoff MI, Sondermann H Structure. 2008 Dec 12;16(12):1817-27. PMID:19081058[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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