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9GUS

30S mRNA delivery complex TEC resolved (30S only)

Summary for 9GUS
Entry DOI10.2210/pdb9gus/pdb
Related9GUR
EMDB information51618
Descriptor16S ribosomal RNA, 30S ribosomal protein S9, 30S ribosomal protein S10, ... (25 entities in total)
Functional Keywordstranscription, translation, coupling., ribosome
Biological sourceEscherichia coli K-12
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Total number of polymer chains24
Total formula weight891436.90
Authors
Rahil, H.,Weixlbaumer, A.,Webster, M.W. (deposition date: 2024-09-20, release date: 2024-11-20, Last modification date: 2024-12-11)
Primary citationWebster, M.W.,Chauvier, A.,Rahil, H.,Graziadei, A.,Charles, K.,Miropolskaya, N.,Takacs, M.,Saint-Andre, C.,Rappsilber, J.,Walter, N.G.,Weixlbaumer, A.
Molecular basis of mRNA delivery to the bacterial ribosome.
Science, 386:eado8476-eado8476, 2024
Cited by
PubMed Abstract: Protein synthesis begins with the formation of a ribosome-messenger RNA (mRNA) complex. In bacteria, the small ribosomal subunit (30) is recruited to many mRNAs through base pairing with the Shine-Dalgarno (SD) sequence and RNA binding by ribosomal protein bS1. Translation can initiate on nascent mRNAs, and RNA polymerase (RNAP) can promote the recruitment of the pioneering 30. Here, we examined 30 recruitment to nascent mRNAs using cryo-electron microscopy, single-molecule fluorescence colocalization, and in-cell cross-linking mass spectrometry. We show that bS1 delivers the mRNA to the ribosome for SD duplex formation and 30 activation. Additionally, bS1 and RNAP stimulate translation initiation. Our work provides a mechanistic framework for how the SD duplex, ribosomal proteins, and RNAP cooperate in 30 recruitment to mRNAs and establish transcription-translation coupling.
PubMed: 39607923
DOI: 10.1126/science.ado8476
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.5 Å)
Structure validation

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