Summary for 7BHP
| Entry DOI | 10.2210/pdb7bhp/pdb |
| EMDB information | 12189 |
| Descriptor | 28S ribosomal RNA, 60S ribosomal protein L7a, 60S ribosomal protein L9, ... (48 entities in total) |
| Functional Keywords | ebp1, pag2g4, metap2, metalloprotease, ribosome, es27, ribosomal tunnel exit |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 45 |
| Total formula weight | 2595971.49 |
| Authors | Desogus, J.,Bhaskar, V.,Chao, J.A. (deposition date: 2021-01-11, release date: 2021-02-03, Last modification date: 2024-11-06) |
| Primary citation | Bhaskar, V.,Desogus, J.,Graff-Meyer, A.,Schenk, A.D.,Cavadini, S.,Chao, J.A. Dynamic association of human Ebp1 with the ribosome. Rna, 27:411-419, 2021 Cited by PubMed Abstract: Ribosomes are the macromolecular machines at the heart of protein synthesis; however, their function can be modulated by a variety of additional protein factors that directly interact with them. Here, we report the cryo-EM structure of human Ebp1 (p48 isoform) bound to the human 80S ribosome at 3.3 Å resolution. Ebp1 binds in the vicinity of the peptide exit tunnel on the 80S ribosome, and this binding is enhanced upon puromycin-mediated translational inhibition. The association of Ebp1 with the 80S ribosome centers around its interaction with ribosomal proteins eL19 and uL23 and the 28S rRNA. Further analysis of the Ebp1-ribosome complex suggests that Ebp1 can rotate around its insert domain, which may enable it to assume a wide range of conformations while maintaining its interaction with the ribosome. Structurally, Ebp1 shares homology with the methionine aminopeptidase 2 family of enzymes; therefore, this inherent flexibility may also be conserved. PubMed: 33479117DOI: 10.1261/rna.077602.120 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.3 Å) |
Structure validation
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