3w1d: Difference between revisions
New page: '''Unreleased structure''' The entry 3w1d is ON HOLD Authors: Imada, K., Yoshizawa, K., Kinoshita, M., Watanabe, T.M. Description: Structure of a pressure sensitive YFP variant YFP-G3 |
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The entry | ==Structure of a pressure sensitive YFP variant YFP-G3== | ||
<StructureSection load='3w1d' size='340' side='right'caption='[[3w1d]], [[Resolution|resolution]] 1.50Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3w1d]] 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=3W1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W1D FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CR2:{(4Z)-2-(AMINOMETHYL)-4-[(4-HYDROXYPHENYL)METHYLIDENE]-5-OXO-4,5-DIHYDRO-1H-IMIDAZOL-1-YL}ACETIC+ACID'>CR2</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=3w1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w1d OCA], [https://pdbe.org/3w1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w1d RCSB], [https://www.ebi.ac.uk/pdbsum/3w1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w1d ProSAT]</span></td></tr> | |||
</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. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Fluorescent protein-based indicators for intracellular environment conditions such as pH and ion concentrations are commonly used to study the status and dynamics of living cells. Despite being an important factor in many biological processes, the development of an indicator for the physicochemical state of water, such as pressure, viscosity and temperature, however, has been neglected. We here found a novel mutation that dramatically enhances the pressure dependency of the yellow fluorescent protein (YFP) by inserting several glycines into it. The crystal structure of the mutant showed that the tyrosine near the chromophore flipped toward the outside of the beta-can structure, resulting in the entry of a few water molecules near the chromophore. In response to changes in hydrostatic pressure, a spectrum shift and an intensity change of the fluorescence were observed. By measuring the fluorescence of the YFP mutant, we succeeded in measuring the intracellular pressure change in living cell. This study shows a new strategy of design to engineer fluorescent protein indicators to sense hydrostatic pressure. | |||
Glycine insertion makes yellow fluorescent protein sensitive to hydrostatic pressure.,Watanabe TM, Imada K, Yoshizawa K, Nishiyama M, Kato C, Abe F, Morikawa TJ, Kinoshita M, Fujita H, Yanagida T PLoS One. 2013 Aug 27;8(8):e73212. doi: 10.1371/journal.pone.0073212. PMID:24014139<ref>PMID:24014139</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 3w1d" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Aequorea victoria]] | |||
[[Category: Large Structures]] | |||
[[Category: Imada K]] | |||
[[Category: Kinoshita M]] | |||
[[Category: Watanabe TM]] | |||
[[Category: Yoshizawa K]] | |||
Latest revision as of 15:45, 8 November 2023
Structure of a pressure sensitive YFP variant YFP-G3Structure of a pressure sensitive YFP variant YFP-G3
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 PubMedFluorescent protein-based indicators for intracellular environment conditions such as pH and ion concentrations are commonly used to study the status and dynamics of living cells. Despite being an important factor in many biological processes, the development of an indicator for the physicochemical state of water, such as pressure, viscosity and temperature, however, has been neglected. We here found a novel mutation that dramatically enhances the pressure dependency of the yellow fluorescent protein (YFP) by inserting several glycines into it. The crystal structure of the mutant showed that the tyrosine near the chromophore flipped toward the outside of the beta-can structure, resulting in the entry of a few water molecules near the chromophore. In response to changes in hydrostatic pressure, a spectrum shift and an intensity change of the fluorescence were observed. By measuring the fluorescence of the YFP mutant, we succeeded in measuring the intracellular pressure change in living cell. This study shows a new strategy of design to engineer fluorescent protein indicators to sense hydrostatic pressure. Glycine insertion makes yellow fluorescent protein sensitive to hydrostatic pressure.,Watanabe TM, Imada K, Yoshizawa K, Nishiyama M, Kato C, Abe F, Morikawa TJ, Kinoshita M, Fujita H, Yanagida T PLoS One. 2013 Aug 27;8(8):e73212. doi: 10.1371/journal.pone.0073212. PMID:24014139[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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