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4YB0

3',3'-cGAMP riboswitch bound with c-di-GMP

Summary for 4YB0
Entry DOI10.2210/pdb4yb0/pdb
Related4YAZ 4YB1
DescriptorRNA (84-MER), GUANOSINE-5'-DIPHOSPHATE, 9,9'-[(2R,3R,3aS,5S,7aR,9R,10R,10aS,12S,14aR)-3,5,10,12-tetrahydroxy-5,12-dioxidooctahydro-2H,7H-difuro[3,2-d:3',2'-j][1,3,7,9,2,8]tetraoxadiphosphacyclododecine-2,9-diyl]bis(2-amino-1,9-dihydro-6H-purin-6-one), ... (6 entities in total)
Functional Keywordsriboswitch, 3', 3'-cgamp, spinach, rna structure, c-di-gmp, rna
Biological sourceGeobacter
Total number of polymer chains2
Total formula weight56135.13
Authors
Ren, A.M.,Patel, D.J.,Rajashankar, R.K. (deposition date: 2015-02-18, release date: 2015-04-15, Last modification date: 2023-09-27)
Primary citationRen, A.,Wang, X.C.,Kellenberger, C.A.,Rajashankar, K.R.,Jones, R.A.,Hammond, M.C.,Patel, D.J.
Structural Basis for Molecular Discrimination by a 3',3'-cGAMP Sensing Riboswitch.
Cell Rep, 11:1-12, 2015
Cited by
PubMed Abstract: Cyclic dinucleotides are second messengers that target the adaptor STING and stimulate the innate immune response in mammals. Besides protein receptors, there are bacterial riboswitches that selectively recognize cyclic dinucleotides. We recently discovered a natural riboswitch that targets 3',3'-cGAMP, which is distinguished from the endogenous mammalian signal 2',3'-cGAMP by its backbone connectivity. Here, we report on structures of the aptamer domain of the 3',3'-cGAMP riboswitch from Geobacter in the 3',3'-cGAMP and c-di-GMP bound states. The riboswitch adopts a tuning fork-like architecture with a junctional ligand-binding pocket and different orientations of the arms are correlated with the identity of the bound cyclic dinucleotide. Subsequent biochemical experiments revealed that specificity of ligand recognition can be affected by point mutations outside of the binding pocket, which has implications for both the assignment and reengineering of riboswitches in this structural class.
PubMed: 25818298
DOI: 10.1016/j.celrep.2015.03.004
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.121 Å)
Structure validation

226707

數據於2024-10-30公開中

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