4LX5
X-ray crystal structure of the M6" riboswitch aptamer bound to pyrimido[4,5-d]pyrimidine-2,4-diamine (PPDA)
Summary for 4LX5
Entry DOI | 10.2210/pdb4lx5/pdb |
Related | 3LA5 4LX6 |
Descriptor | Mutated adenine riboswitch aptamer, pyrimido[4,5-d]pyrimidine-2,4-diamine, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | riboswitch, gene expression platform, rna |
Biological source | Vibrio vulnificus |
Total number of polymer chains | 1 |
Total formula weight | 22944.79 |
Authors | Dunstan, M.S.,Leys, D. (deposition date: 2013-07-29, release date: 2014-07-16, Last modification date: 2023-09-20) |
Primary citation | Robinson, C.J.,Vincent, H.A.,Wu, M.C.,Lowe, P.T.,Dunstan, M.S.,Leys, D.,Micklefield, J. Modular riboswitch toolsets for synthetic genetic control in diverse bacterial species. J.Am.Chem.Soc., 136:10615-10624, 2014 Cited by PubMed Abstract: Ligand-dependent control of gene expression is essential for gene functional analysis, target validation, protein production, and metabolic engineering. However, the expression tools currently available are difficult to transfer between species and exhibit limited mechanistic diversity. Here we demonstrate how the modular architecture of purine riboswitches can be exploited to develop orthogonal and chimeric switches that are transferable across diverse bacterial species, modulating either transcription or translation, to provide tunable activation or repression of target gene expression, in response to synthetic non-natural effector molecules. Our novel riboswitch-ligand pairings are shown to regulate physiologically important genes required for bacterial motility in Escherichia coli and cell morphology in Bacillus subtilis. These findings are relevant for future gene function studies and antimicrobial target validation, while providing new modular and orthogonal regulatory components for deployment in synthetic biology regimes. PubMed: 24971878DOI: 10.1021/ja502873j PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
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