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5JVA

1.95 angstrom crystal structure of TAGRFP-T

Replaces:  3T6H
Summary for 5JVA
Entry DOI10.2210/pdb5jva/pdb
Related3T6H
DescriptorTagRFP-T, BETA-MERCAPTOETHANOL, SULFATE ION, ... (4 entities in total)
Functional Keywordsred fluorescent proteins, tagrfp-t, beta barrel, photostable, fluorescent protein
Biological sourcesynthetic construct
Total number of polymer chains4
Total formula weight109116.31
Authors
Hu, X.J. (deposition date: 2016-05-11, release date: 2017-05-17, Last modification date: 2024-04-03)
Primary citationLiu, R.,Liang, Q.N.,Du, S.Q.,Hu, X.J.,Ding, Y.
The crystal structure of red fluorescent protein TagRFP-T reveals the mechanism of its superior photostability.
Biochem. Biophys. Res. Commun., 477:229-234, 2016
Cited by
PubMed Abstract: The red fluorescent protein variant TagRFP-T has greatly improved photostability over its parent molecule, TagRFP, but the underlying mechanism leading to this improvement is to date unknown. The 1.95 Å resolution crystallographic structure of TagRFP-T showed that its chromophore exists as a mixture of cis and trans coplanar isomers in roughly equal proportions. Interestingly, both isomers are able to fluoresce, a property that has never been observed in any other fluorescent protein. We propose a "circular restoration model" for TagRFP-T to explain its superior photostability: There are four co-existing chromophore states (cis/trans protonated/ionized state) that can be driven by light to transform from one state into another. This model also explains how TagRPF-T essentially eliminates the temporary dark state (reversible photobleaching).
PubMed: 27297107
DOI: 10.1016/j.bbrc.2016.06.047
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.95 Å)
Structure validation

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