Summary for 4V7R
Entry DOI | 10.2210/pdb4v7r/pdb |
Descriptor | 18S ribosomal RNA, 40S ribosomal protein S15, 40S ribosomal protein S16, ... (74 entities in total) |
Functional Keywords | ribosomal rrna and proteins, translating the genetic code to proteins, ribosome, eukaryotic, yeast |
Biological source | Saccharomyces cerevisiae (yeast) More |
Cellular location | Cytoplasm : Q01855 P02407 P07280 P38701 P0C0W1 Q3E792 Q3E7X9 P32905 P41057 P38011 P25443 P14126 P10664 P26321 Q02326 P05737 P17076 P05750 P05738 P41805 P0C0W9 P36105 P05748 P26784 P05740 Q02753 P26783 P04449 P04456 P05743 P02406 P14120 P0C2H8 P38061 P49166 O13516 P04650 P05756 P05317 P06367 |
Total number of polymer chains | 139 |
Total formula weight | 5851649.47 |
Authors | Ben-Shem, A.,Jenner, L.,Yusupova, G.,Yusupov, M. (deposition date: 2010-07-23, release date: 2014-07-09, Last modification date: 2024-02-28) |
Primary citation | Ben-Shem, A.,Jenner, L.,Yusupova, G.,Yusupov, M. Crystal structure of the eukaryotic ribosome. Science, 330:1203-1209, 2010 Cited by PubMed Abstract: Crystal structures of prokaryotic ribosomes have described in detail the universally conserved core of the translation mechanism. However, many facets of the translation process in eukaryotes are not shared with prokaryotes. The crystal structure of the yeast 80S ribosome determined at 4.15 angstrom resolution reveals the higher complexity of eukaryotic ribosomes, which are 40% larger than their bacterial counterparts. Our model shows how eukaryote-specific elements considerably expand the network of interactions within the ribosome and provides insights into eukaryote-specific features of protein synthesis. Our crystals capture the ribosome in the ratcheted state, which is essential for translocation of mRNA and transfer RNA (tRNA), and in which the small ribosomal subunit has rotated with respect to the large subunit. We describe the conformational changes in both ribosomal subunits that are involved in ratcheting and their implications in coordination between the two associated subunits and in mRNA and tRNA translocation. PubMed: 21109664DOI: 10.1126/science.1194294 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4 Å) |
Structure validation
Download full validation report
