2gis

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(New page: 200px<br /><applet load="2gis" size="350" color="white" frame="true" align="right" spinBox="true" caption="2gis, resolution 2.90&Aring;" /> '''Structure of the S-a...)
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Revision as of 18:00, 29 January 2008


2gis, resolution 2.90Å

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Structure of the S-adenosylmethionine riboswitch mRNA regulatory element

Overview

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.

About this Structure

2GIS is a Protein complex structure of sequences from [1] with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the S-adenosylmethionine riboswitch regulatory mRNA element., Montange RK, Batey RT, Nature. 2006 Jun 29;441(7097):1172-5. PMID:16810258

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