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7AV6

FAST in a domain-swapped dimer form

Summary for 7AV6
Entry DOI10.2210/pdb7av6/pdb
DescriptorPhotoactive yellow protein, FORMIC ACID (3 entities in total)
Functional Keywordsfluorescence, fluorogen, fluorogen-activating protein, fluorescent labelling, fast, fluorescent protein
Biological sourceHalorhodospira halophila
Total number of polymer chains1
Total formula weight15341.22
Authors
Bukhdruker, S.,Remeeva, A.,Ruchkin, D.,Gorbachev, D.,Povarova, N.,Mineev, K.,Goncharuk, S.,Baranov, M.,Mishin, A.,Borshchevskiy, V. (deposition date: 2020-11-04, release date: 2021-06-09, Last modification date: 2024-01-31)
Primary citationMineev, K.S.,Goncharuk, S.A.,Goncharuk, M.V.,Povarova, N.V.,Sokolov, A.I.,Baleeva, N.S.,Smirnov, A.Y.,Myasnyanko, I.N.,Ruchkin, D.A.,Bukhdruker, S.,Remeeva, A.,Mishin, A.,Borshchevskiy, V.,Gordeliy, V.,Arseniev, A.S.,Gorbachev, D.A.,Gavrikov, A.S.,Mishin, A.S.,Baranov, M.S.
NanoFAST: structure-based design of a small fluorogen-activating protein with only 98 amino acids.
Chem Sci, 12:6719-6725, 2021
Cited by
PubMed Abstract: One of the essential characteristics of any tag used in bioscience and medical applications is its size. The larger the label, the more it may affect the studied object, and the more it may distort its behavior. In this paper, using NMR spectroscopy and X-ray crystallography, we have studied the structure of fluorogen-activating protein FAST both in the apo form and in complex with the fluorogen. We showed that significant change in the protein occurs upon interaction with the ligand. While the protein is completely ordered in the complex, its apo form is characterized by higher mobility and disordering of its N-terminus. We used structural information to design the shortened FAST (which we named nanoFAST) by truncating 26 N-terminal residues. Thus, we created the shortest genetically encoded tag among all known fluorescent and fluorogen-activating proteins, which is composed of only 98 amino acids.
PubMed: 34040747
DOI: 10.1039/d1sc01454d
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.5 Å)
Structure validation

226707

건을2024-10-30부터공개중

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