7pca: Difference between revisions
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<StructureSection load='7pca' size='340' side='right'caption='[[7pca]], [[Resolution|resolution]] 1.05Å' scene=''> | <StructureSection load='7pca' size='340' side='right'caption='[[7pca]], [[Resolution|resolution]] 1.05Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7pca]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PCA FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pca]] 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=7PCA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PCA FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARF:FORMAMIDE'>ARF</scene>, | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ARF:FORMAMIDE'>ARF</scene>, <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>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=7pca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pca OCA], [https://pdbe.org/7pca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pca RCSB], [https://www.ebi.ac.uk/pdbsum/7pca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pca 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=7pca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pca OCA], [https://pdbe.org/7pca PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pca RCSB], [https://www.ebi.ac.uk/pdbsum/7pca PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pca 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. | [[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: Aequorea victoria]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Becker | [[Category: Becker K]] | ||
[[Category: Fritz-Wolf | [[Category: Fritz-Wolf K]] | ||
[[Category: Heimsch | [[Category: Heimsch KC]] | ||
[[Category: Schuh | [[Category: Schuh AK]] | ||
Revision as of 08:25, 8 September 2022
Functional and structural characterization of redox sensitive superfolder green fluorescent protein and variantsFunctional and structural characterization of redox sensitive superfolder green fluorescent protein and variants
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. Publication Abstract from PubMedAIMS: Genetically encoded GFP-based redox biosensors are widely used to monitor specific and dynamic redox processes in living cells. Over the last years, various biosensors for a variety of applications were engineered and enhanced to match the organism and cellular environments, which should be investigated. In this context, the unicellular intraerythrocytic parasite Plasmodium, the causative agent of malaria, represents a challenge, as the small size of the organism results in weak fluorescence signals that complicate precise measurements, especially for cell compartment-specific observations. To address this, we have functionally and structurally characterized an enhanced redox biosensor superfolder roGFP2 (sfroGFP2). RESULTS: SfroGFP2 retains roGFP2-like behavior, yet with improved fluorescence intensity in cellulo. SfroGFP2-based redox biosensors are pH-insensitive in a physiological pH range and show midpoint potentials comparable to roGFP2-based redox biosensors. Using crystallography and rigidity theory, we identified the superfolding mutations as being responsible for improved structural stability of the biosensor in a redox-sensitive environment, thus explaining the improved fluorescence intensity in cellulo. INNOVATION: This work provides insight into the structure and function of GFP-based redox biosensors. It describes an improved redox biosensor (sfroGFP2) suitable for measuring oxidizing effects within small cells where applicability of other redox sensor variants is limited. CONCLUSION: Improved structural stability of sfroGFP2 gives rise to increased fluorescence intensity in cellulo. Fusion to hGrx1 provides the hitherto most suitable biosensor for measuring oxidizing effects in Plasmodium. This sensor is of major interest for studying glutathione redox changes in small cells, as well as subcellular compartments in general. Structure and function of redox-sensitive superfolder green fluorescent protein variant.,Heimsch K, Gertzen CW, Schuh K, Nietzel T, Rahlfs S, Przyborski J, Gohlke H, Schwarzlander M, Becker K, Fritz-Wolf K Antioxid Redox Signal. 2022 Jan 24. doi: 10.1089/ars.2021.0234. PMID:35072524[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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