2QWY
SAM-II riboswitch bound to S-adenosylmethionine
Summary for 2QWY
| Entry DOI | 10.2210/pdb2qwy/pdb |
| Descriptor | SAM-II riboswitch, PHOSPHATE ION, CESIUM ION, ... (6 entities in total) |
| Functional Keywords | mrna, riboswitch, sam, s-adenosylmethionine, adomet, rna-ligand complex, double helix, pseudoknot, base triple, rna |
| Total number of polymer chains | 3 |
| Total formula weight | 52518.38 |
| Authors | Gilbert, S.D.,Rambo, R.P.,Van Tyne, D.,Batey, R.T. (deposition date: 2007-08-10, release date: 2008-01-22, Last modification date: 2024-02-21) |
| Primary citation | Gilbert, S.D.,Rambo, R.P.,Van Tyne, D.,Batey, R.T. Structure of the SAM-II riboswitch bound to S-adenosylmethionine. Nat.Struct.Mol.Biol., 15:177-182, 2008 Cited by PubMed Abstract: In bacteria, numerous genes harbor regulatory elements in the 5' untranslated regions of their mRNA, termed riboswitches, which control gene expression by binding small-molecule metabolites. These sequences influence the secondary and tertiary structure of the RNA in a ligand-dependent manner, thereby directing its transcription or translation. The crystal structure of an S-adenosylmethionine-responsive riboswitch found predominantly in proteobacteria, SAM-II, has been solved to reveal a second means by which RNA interacts with this important cellular metabolite. Notably, this is the first structure of a complete riboswitch containing all sequences associated with both the ligand binding aptamer domain and the regulatory expression platform. Chemical probing of this RNA in the absence and presence of ligand shows how the structure changes in response to S-adenosylmethionine to sequester the ribosomal binding site and affect translational gene regulation. PubMed: 18204466DOI: 10.1038/nsmb.1371 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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