PMID:11593008

Citation	Sengupta, J, Agrawal, RK and Frank, J (2001) Visualization of protein S1 within the 30S ribosomal subunit and its interaction with messenger RNA. Proc. Natl. Acad. Sci. U.S.A. 98:11991-6
Abstract	S1 is the largest ribosomal protein, present in the small subunit of the bacterial ribosome. It has a pivotal role in stabilizing the mRNA on the ribosome. Thus far, S1 has eluded structural determination. We have identified the S1 protein mass in the cryo-electron microscopic map of the Escherichia coli ribosome by comparing the map with a recent x-ray crystallographic structure of the 30S subunit, which lacks S1. According to our finding, S1 is located at the junction of head, platform, and main body of the 30S subunit, thus explaining all existing biochemical and crosslinking data. Protein S1 as identified in our map has a complex, elongated shape with two holes in its central portion. The N-terminal domain, forming one of the extensions, penetrates into the head of the 30S subunit. Evidence for direct interaction of S1 with 11 nucleotides of the mRNA, immediately upstream of the Shine-Dalgarno sequence, explains the protein's role in the recognition of the 5' region of mRNA.
Links	PubMed PMC59823 Online version:10.1073/pnas.211266898
Keywords	Cryoelectron Microscopy/methods; Models, Molecular; Protein Structure, Tertiary; RNA, Messenger/chemistry; RNA, Messenger/metabolism; RNA, Ribosomal, 16S/chemistry; RNA, Ribosomal, 16S/metabolism; Ribosomal Proteins/chemistry; Ribosomal Proteins/metabolism; Ribosomes/metabolism; Thermus thermophilus
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