4V5O

CRYSTAL STRUCTURE OF THE EUKARYOTIC 40S RIBOSOMAL SUBUNIT IN COMPLEX WITH INITIATION FACTOR 1.

This is a non-PDB format compatible entry.

Summary for 4V5O

• Entry DOI: 10.2210/pdb4v5o/pdb
• Descriptor: RIBOSOMAL PROTEIN S28E CONTAINING PROTEIN, 18S RRNA, RPS0E, ... (38 entities in total)
• Functional Keywords: ribosome, translation
• Biological source: TETRAHYMENA THERMOPHILA; More
• Cellular location: Cytoplasm : 4V5O
• Total number of polymer chains: 70
• Total formula weight: 2424398.83

Authors

Rabl, J.,Leibundgut, M.,Ataide, S.F.,Haag, A.,Ban, N. (deposition date: 2010-11-26, release date: 2014-07-09, Last modification date: 2024-11-06)

Primary citation

Rabl, J.,Leibundgut, M.,Ataide, S.F.,Haag, A.,Ban, N.
Crystal Structure of the Eukaryotic 40S Ribosomal Subunit in Complex with Initiation Factor 1.
Science, 331:730-, 2011

PubMed Abstract: Eukaryotic ribosomes are substantially larger and more complex than their bacterial counterparts. Although their core function is conserved, bacterial and eukaryotic protein synthesis differ considerably at the level of initiation. The eukaryotic small ribosomal subunit (40S) plays a central role in this process; it binds initiation factors that facilitate scanning of messenger RNAs and initiation of protein synthesis. We have determined the crystal structure of the Tetrahymena thermophila 40S ribosomal subunit in complex with eukaryotic initiation factor 1 (eIF1) at a resolution of 3.9 angstroms. The structure reveals the fold of the entire 18S ribosomal RNA and of all ribosomal proteins of the 40S subunit, and defines the interactions with eIF1. It provides insights into the eukaryotic-specific aspects of protein synthesis, including the function of eIF1 as well as signaling and regulation mediated by the ribosomal proteins RACK1 and rpS6e.

PubMed: 21205638
DOI: 10.1126/SCIENCE.1198308

Experimental method

X-RAY DIFFRACTION (3.93 Å)