3EQ4
Model of tRNA(Leu)-EF-Tu in the ribosomal pre-accommodated state revealed by cryo-EM
Summary for 3EQ4
Entry DOI | 10.2210/pdb3eq4/pdb |
Related | 1OB2 1QZA 2AVY 2AW4 3EP2 3EQ3 |
EMDB information | 1564 1565 |
Descriptor | Elongation factor Tu, 30S ribosomal protein S12, 50S ribosomal protein L11, ... (9 entities in total) |
Functional Keywords | protein translation, ternary complex, a/t-trna, automated data collection, antibiotic resistance, elongation factor, gtp-binding, membrane, methylation, nucleotide-binding, phosphoprotein, protein biosynthesis, ribonucleoprotein, ribosomal protein, rna-binding, rrna-binding, trna-binding, ribosomal protein-rna complex, ribosomal protein/rna |
Biological source | Escherichia coli K12 More |
Total number of polymer chains | 9 |
Total formula weight | 135481.63 |
Authors | Frank, J.,Li, W.,Agirrezabala, X. (deposition date: 2008-09-30, release date: 2008-12-16, Last modification date: 2024-02-21) |
Primary citation | Li, W.,Agirrezabala, X.,Lei, J.,Bouakaz, L.,Brunelle, J.L.,Ortiz-Meoz, R.F.,Green, R.,Sanyal, S.,Ehrenberg, M.,Frank, J. Recognition of aminoacyl-tRNA: a common molecular mechanism revealed by cryo-EM. Embo J., 27:3322-3331, 2008 Cited by PubMed: 19020518DOI: 10.1038/emboj.2008.243 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (12 Å) |
Structure validation
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