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| | <StructureSection load='7pcz' size='340' side='right'caption='[[7pcz]], [[Resolution|resolution]] 1.35Å' scene=''> | | <StructureSection load='7pcz' size='340' side='right'caption='[[7pcz]], [[Resolution|resolution]] 1.35Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7pcz]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PCZ FirstGlance]. <br> | + | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7PCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PCZ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.35Å</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> | + | <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>, <scene name='pdbligand=EOH:ETHANOL'>EOH</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[7pca|7pca]]</div></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=7pcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pcz OCA], [https://pdbe.org/7pcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pcz RCSB], [https://www.ebi.ac.uk/pdbsum/7pcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pcz 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=7pcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pcz OCA], [https://pdbe.org/7pcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pcz RCSB], [https://www.ebi.ac.uk/pdbsum/7pcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pcz 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. | |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 7pcz" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 7pcz" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Green Fluorescent Protein 3D structures|Green Fluorescent Protein 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Becker, K]] | + | [[Category: Becker K]] |
| - | [[Category: Fritz-Wolf, K]] | + | [[Category: Fritz-Wolf K]] |
| - | [[Category: Heimsch, K C]] | + | [[Category: Heimsch KC]] |
| - | [[Category: Schuh, A K]] | + | [[Category: Schuh AK]] |
| - | [[Category: Dynamic simulation]]
| + | |
| - | [[Category: Fluorescent protein]]
| + | |
| - | [[Category: Genetically encoded biosensor]]
| + | |
| - | [[Category: Plasmodium falciparum]]
| + | |
| - | [[Category: Redox regulation]]
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| - | [[Category: X-ray crystal structure]]
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| Structural highlights
Publication Abstract from PubMed
AIMS: 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.
See Also
References
- ↑ Heimsch K, Gertzen CW, Schuh K, Nietzel T, Rahlfs S, Przyborski J, Gohlke H, Schwarzlander M, Becker K, Fritz-Wolf K. Structure and function of redox-sensitive superfolder green fluorescent protein variant. Antioxid Redox Signal. 2022 Jan 24. doi: 10.1089/ars.2021.0234. PMID:35072524 doi:http://dx.doi.org/10.1089/ars.2021.0234
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