2GIS
Structure of the S-adenosylmethionine riboswitch mRNA regulatory element
Summary for 2GIS
| Entry DOI | 10.2210/pdb2gis/pdb |
| Descriptor | SAM-I riboswitch, MAGNESIUM ION, IRIDIUM HEXAMMINE ION, ... (5 entities in total) |
| Functional Keywords | mrna, riboswitch, s-adenosylmethionine, sam, rna-ligand complex, rna |
| Total number of polymer chains | 1 |
| Total formula weight | 32177.97 |
| Authors | Montange, R.K.,Batey, R.T. (deposition date: 2006-03-29, release date: 2006-07-04, Last modification date: 2024-02-14) |
| Primary citation | Montange, R.K.,Batey, R.T. Structure of the S-adenosylmethionine riboswitch regulatory mRNA element. Nature, 441:1172-1175, 2006 Cited by PubMed Abstract: Riboswitches are cis-acting genetic regulatory elements found in the 5'-untranslated regions of messenger RNAs that control gene expression through their ability to bind small molecule metabolites directly. Regulation occurs through the interplay of two domains of the RNA: an aptamer domain that responds to intracellular metabolite concentrations and an expression platform that uses two mutually exclusive secondary structures to direct a decision-making process. In Gram-positive bacteria such as Bacillus species, riboswitches control the expression of more than 2% of all genes through their ability to respond to a diverse set of metabolites including amino acids, nucleobases and protein cofactors. Here we report the 2.9-angstroms resolution crystal structure of an S-adenosylmethionine (SAM)-responsive riboswitch from Thermoanaerobacter tengcongensis complexed with S-adenosylmethionine, an RNA element that controls the expression of several genes involved in sulphur and methionine metabolism. This RNA folds into a complex three-dimensional architecture that recognizes almost every functional group of the ligand through a combination of direct and indirect readout mechanisms. Ligand binding induces the formation of a series of tertiary interactions with one of the helices, serving as a communication link between the aptamer and expression platform domains. PubMed: 16810258DOI: 10.1038/nature04819 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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