4V8Z
Cryo-EM reconstruction of the 80S-eIF5B-Met-itRNAMet Eukaryotic Translation Initiation Complex
This is a non-PDB format compatible entry.
Summary for 4V8Z
| Entry DOI | 10.2210/pdb4v8z/pdb |
| Related | 4BYL 4BYN 4BYO 4BYP 4BYQ 4BYR 4BYS |
| EMDB information | 2422 |
| Descriptor | 40S RIBOSOMAL PROTEIN S26-A, 40S RIBOSOMAL PROTEIN S1-A, 40S RIBOSOMAL PROTEIN S2, ... (89 entities in total) |
| Functional Keywords | ribosome, ribosome initiation complex, initiator factor eif5b, single particle analysis |
| Biological source | SACCHAROMYCES CEREVISIAE More |
| Total number of polymer chains | 85 |
| Total formula weight | 3331418.55 |
| Authors | Fernandez, I.S.,Bai, X.C.,Hussain, T.,Kelley, A.C.,Lorsch, J.R.,Ramakrishnan, V.,Scheres, S.H.W. (deposition date: 2013-07-20, release date: 2014-07-09, Last modification date: 2024-11-13) |
| Primary citation | Fernandez, I.S.,Bai, X.C.,Hussain, T.,Kelley, A.C.,Lorsch, J.R.,Ramakrishnan, V.,Scheres, S.H.W. Molecular architecture of a eukaryotic translational initiation complex. Science, 342:1240585-1240585, 2013 Cited by PubMed Abstract: The last step in eukaryotic translational initiation involves the joining of the large and small subunits of the ribosome, with initiator transfer RNA (Met-tRNA(i)(Met)) positioned over the start codon of messenger RNA in the P site. This step is catalyzed by initiation factor eIF5B. We used recent advances in cryo-electron microscopy (cryo-EM) to determine a structure of the eIF5B initiation complex to 6.6 angstrom resolution from <3% of the population, comprising just 5143 particles. The structure reveals conformational changes in eIF5B, initiator tRNA, and the ribosome that provide insights into the role of eIF5B in translational initiation. The relatively high resolution obtained from such a small fraction of a heterogeneous sample suggests a general approach for characterizing the structure of other dynamic or transient biological complexes. PubMed: 24200810DOI: 10.1126/science.1240585 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.6 Å) |
Structure validation
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