6QNR

70S ribosome elongation complex (EC) with experimentally assigned potassium ions

This is a non-PDB format compatible entry.

Summary for 6QNR

• Entry DOI: 10.2210/pdb6qnr/pdb
• Descriptor: 16S ribosomal RNA, 30S ribosomal protein S10, 30S ribosomal protein S11, ... (65 entities in total)
• Functional Keywords: potassium, magnesium, decoding center, rrna, ribosomal proteins, ribosome
• Biological source: Thermus thermophilus HB8; More
• Total number of polymer chains: 114
• Total formula weight: 4648140.68

Authors

Rozov, A.,Khusainov, I.,Yusupov, M.,Yusupova, G. (deposition date: 2019-02-11, release date: 2019-06-19, Last modification date: 2025-03-19)

Primary citation

Rozov, A.,Khusainov, I.,El Omari, K.,Duman, R.,Mykhaylyk, V.,Yusupov, M.,Westhof, E.,Wagner, A.,Yusupova, G.
Importance of potassium ions for ribosome structure and function revealed by long-wavelength X-ray diffraction.
Nat Commun, 10:2519-2519, 2019

PubMed Abstract: The ribosome, the largest RNA-containing macromolecular machinery in cells, requires metal ions not only to maintain its three-dimensional fold but also to perform protein synthesis. Despite the vast biochemical data regarding the importance of metal ions for efficient protein synthesis and the increasing number of ribosome structures solved by X-ray crystallography or cryo-electron microscopy, the assignment of metal ions within the ribosome remains elusive due to methodological limitations. Here we present extensive experimental data on the potassium composition and environment in two structures of functional ribosome complexes obtained by measurement of the potassium anomalous signal at the K-edge, derived from long-wavelength X-ray diffraction data. We elucidate the role of potassium ions in protein synthesis at the three-dimensional level, most notably, in the environment of the ribosome functional decoding and peptidyl transferase centers. Our data expand the fundamental knowledge of the mechanism of ribosome function and structural integrity.

PubMed: 31175275
DOI: 10.1038/s41467-019-10409-4

Experimental method

X-RAY DIFFRACTION (3.1 Å)