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5BJP

Crystal structure of the Corn RNA aptamer in complex with DFHO, iridium hexammine soak

Summary for 5BJP
Entry DOI10.2210/pdb5bjp/pdb
DescriptorRNA (36-MER), IRIDIUM ION, POTASSIUM ION, ... (7 entities in total)
Functional Keywordsaptamer, fluorogenic rna, rna
Biological sourcesynthetic construct
Total number of polymer chains2
Total formula weight24536.98
Authors
Warner, K.D.,Song, W.,Filonov, G.S.,Jaffrey, S.R.,Ferre-D'Amare, A.R. (deposition date: 2016-08-21, release date: 2017-09-27, Last modification date: 2024-03-06)
Primary citationWarner, K.D.,Sjekloca, L.,Song, W.,Filonov, G.S.,Jaffrey, S.R.,Ferre-D'Amare, A.R.
A homodimer interface without base pairs in an RNA mimic of red fluorescent protein.
Nat. Chem. Biol., 13:1195-1201, 2017
Cited by
PubMed Abstract: Corn, a 28-nucleotide RNA, increases yellow fluorescence of its cognate ligand 3,5-difluoro-4-hydroxybenzylidene-imidazolinone-2-oxime (DFHO) by >400-fold. Corn was selected in vitro to overcome limitations of other fluorogenic RNAs, particularly rapid photobleaching. We now report the Corn-DFHO co-crystal structure, discovering that the functional species is a quasisymmetric homodimer. Unusually, the dimer interface, in which six unpaired adenosines break overall two-fold symmetry, lacks any intermolecular base pairs. The homodimer encapsulates one DFHO at its interprotomer interface, sandwiching it with a G-quadruplex from each protomer. Corn and the green-fluorescent Spinach RNA are structurally unrelated. Their convergent use of G-quadruplexes underscores the usefulness of this motif for RNA-induced small-molecule fluorescence. The asymmetric dimer interface of Corn could provide a basis for the development of mutants that only fluoresce as heterodimers. Such variants would be analogous to Split GFP, and may be useful for analyzing RNA co-expression or association, or for designing self-assembling RNA nanostructures.
PubMed: 28945234
DOI: 10.1038/nchembio.2475
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.51 Å)
Structure validation

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