1DV4

PARTIAL STRUCTURE OF 16S RNA OF THE SMALL RIBOSOMAL SUBUNIT FROM THERMUS THERMOPHILUS

Replaces:  1C59

Summary for 1DV4

• Entry DOI: 10.2210/pdb1dv4/pdb
• Descriptor: 16S RIBOSOMAL RNA, RIBOSOMAL PROTEIN S5, RIBOSOMAL PROTEIN S7, ... (4 entities in total)
• Functional Keywords: ribosomes, 30s, thermus thermophilus, 16s rna, ribosome
• Biological source: Thermus thermophilus; More
• Total number of polymer chains: 3
• Total formula weight: 105887.80

Authors

Tocilj, A.,Schlunzen, F.,Janell, D.,Gluhmann, M.,Hansen, H.,Harms, J.,Bashan, A.,Bartels, H.,Agmon, I.,Franceschi, F.,Yonath, A. (deposition date: 2000-01-19, release date: 2000-02-02, Last modification date: 2024-02-07)

Primary citation

Tocilj, A.,Schlunzen, F.,Janell, D.,Gluhmann, M.,Hansen, H.A.,Harms, J.,Bashan, A.,Bartels, H.,Agmon, I.,Franceschi, F.,Yonath, A.
The small ribosomal subunit from Thermus thermophilus at 4.5 A resolution: pattern fittings and the identification of a functional site.
Proc.Natl.Acad.Sci.USA, 96:14252-14257, 1999

PubMed Abstract: The electron density map of the small ribosomal subunit from Thermus thermophilus, constructed at 4.5 A resolution, shows the recognizable morphology of this particle, as well as structural features that were interpreted as ribosomal RNA and proteins. Unbiased assignments, carried out by quantitative covalent binding of heavy atom compounds at predetermined sites, led to the localization of the surface of the ribosomal protein S13 at a position compatible with previous assignments, whereas the surface of S11 was localized at a distance of about twice its diameter from the site suggested for its center by neutron scattering. Proteins S5 and S7, whose structures have been determined crystallographically, were visually placed in the map with no alterations in their conformations. Regions suitable to host the fold of protein S15 were detected in several positions, all at a significant distance from the location of this protein in the neutron scattering map. Targeting the 16S RNA region, where mRNA docks to allow the formation of the initiation complex by a mercurated mRNA analog, led to the characterization of its vicinity.

PubMed: 10588692
DOI: 10.1073/pnas.96.25.14252

Experimental method

X-RAY DIFFRACTION (4.5 Å)