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6ZSN

Crystal structure of rsGCaMP double mutant Ile80His/Val116Ile in the OFF state (illuminated)

Summary for 6ZSN
Entry DOI10.2210/pdb6zsn/pdb
DescriptorGreen fluorescent protein,Green fluorescent protein,Calmodulin, FORMIC ACID, CALCIUM ION, ... (5 entities in total)
Functional Keywordsreversible switchable fluorescent protein, calcium sensor, calmodulin, fluorescent protein
Biological sourceAequorea victoria (Jellyfish)
More
Total number of polymer chains1
Total formula weight47784.44
Authors
Janowski, R.,Fuenzalida-Werner, J.P.,Mishra, K.,Stiel, A.C.,Niessing, D. (deposition date: 2020-07-16, release date: 2021-10-27, Last modification date: 2024-01-31)
Primary citationMishra, K.,Fuenzalida-Werner, J.P.,Pennacchietti, F.,Janowski, R.,Chmyrov, A.,Huang, Y.,Zakian, C.,Klemm, U.,Testa, I.,Niessing, D.,Ntziachristos, V.,Stiel, A.C.
Genetically encoded photo-switchable molecular sensors for optoacoustic and super-resolution imaging.
Nat.Biotechnol., 40:598-605, 2022
Cited by
PubMed Abstract: Reversibly photo-switchable proteins are essential for many super-resolution fluorescence microscopic and optoacoustic imaging methods. However, they have yet to be used as sensors that measure the distribution of specific analytes at the nanoscale or in the tissues of live animals. Here we constructed the prototype of a photo-switchable Ca sensor based on GCaMP5G that can be switched with 405/488-nm light and describe its molecular mechanisms at the structural level, including the importance of the interaction of the core barrel structure of the fluorescent protein with the Ca receptor moiety. We demonstrate super-resolution imaging of Ca concentration in cultured cells and optoacoustic Ca imaging in implanted tumor cells in mice under controlled Ca conditions. Finally, we show the generalizability of the concept by constructing examples of photo-switching maltose and dopamine sensors based on periplasmatic binding protein and G-protein-coupled receptor-based sensors.
PubMed: 34845372
DOI: 10.1038/s41587-021-01100-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

238268

数据于2025-07-02公开中

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