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6POM

Cryo-EM structure of the full-length Bacillus subtilis glyQS T-box riboswitch in complex with tRNA-Gly

Summary for 6POM
Entry DOI10.2210/pdb6pom/pdb
Related6PMO
EMDB information20416
DescriptorT-box GlyQS leader (155-MER), tRNAGly (75-MER) (2 entities in total)
Functional Keywordsrna complex, riboswitch, transcription attenuation, stacking., rna
Biological sourceBacillus subtilis
More
Total number of polymer chains2
Total formula weight78886.89
Authors
Li, S.,Su, Z.,Zhang, J.,Chiu, W. (deposition date: 2019-07-04, release date: 2019-11-20, Last modification date: 2024-03-20)
Primary citationLi, S.,Su, Z.,Lehmann, J.,Stamatopoulou, V.,Giarimoglou, N.,Henderson, F.E.,Fan, L.,Pintilie, G.D.,Zhang, K.,Chen, M.,Ludtke, S.J.,Wang, Y.X.,Stathopoulos, C.,Chiu, W.,Zhang, J.
Structural basis of amino acid surveillance by higher-order tRNA-mRNA interactions.
Nat.Struct.Mol.Biol., 26:1094-1105, 2019
Cited by
PubMed Abstract: Amino acid availability in Gram-positive bacteria is monitored by T-box riboswitches. T-boxes directly bind tRNAs, assess their aminoacylation state, and regulate the transcription or translation of downstream genes to maintain nutritional homeostasis. Here, we report cocrystal and cryo-EM structures of Geobacillus kaustophilus and Bacillus subtilis T-box-tRNA complexes, detailing their multivalent, exquisitely selective interactions. The T-box forms a U-shaped molecular vise that clamps the tRNA, captures its 3' end using an elaborate 'discriminator' structure, and interrogates its aminoacylation state using a steric filter fashioned from a wobble base pair. In the absence of aminoacylation, T-boxes clutch tRNAs and form a continuously stacked central spine, permitting transcriptional readthrough or translation initiation. A modeled aminoacyl disrupts tRNA-T-box stacking, severing the central spine and blocking gene expression. Our data establish a universal mechanism of amino acid sensing on tRNAs and gene regulation by T-box riboswitches and exemplify how higher-order RNA-RNA interactions achieve multivalency and specificity.
PubMed: 31740854
DOI: 10.1038/s41594-019-0326-7
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (4.9 Å)
Structure validation

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