4V9F
The re-refined crystal structure of the Haloarcula marismortui large ribosomal subunit at 2.4 Angstrom resolution: more complete structure of the L7/L12 and L1 stalk, L5 and LX proteins
This is a non-PDB format compatible entry.
Summary for 4V9F
| Entry DOI | 10.2210/pdb4v9f/pdb |
| Related | 1FFK 2QA4 3CC2 3JSY |
| Descriptor | 23S Ribosomal RNA, 50S ribosomal protein L10e, 50S ribosomal protein L11P, ... (40 entities in total) |
| Functional Keywords | 50s ribosomal subunit, ribonucleoprotein, ribosomal protein, rna binding, trna binding, metal binding, ribosome |
| Biological source | Haloarcula marismortui More |
| Total number of polymer chains | 34 |
| Total formula weight | 1486403.17 |
| Authors | Gabdulkhakov, A. (deposition date: 2012-11-02, release date: 2014-07-09, Last modification date: 2023-09-20) |
| Primary citation | Gabdulkhakov, A.,Nikonov, S.,Garber, M. Revisiting the Haloarcula marismortui 50S ribosomal subunit model. Acta Crystallogr.,Sect.D, 69:997-1004, 2013 Cited by PubMed Abstract: The structure of the large ribosomal subunit from the halophilic archaeon Haloarcula marismortui (Hma) is the only crystal structure of an archaeal ribosomal particle that has been determined to date. However, the first model of the Hma 50S ribosomal subunit contained some gaps: the structures of functionally important mobile lateral protuberances were not visualized. Subsequently, some parts of the P (L12) stalk base were visualized at 3.0 Å resolution [Kavran & Steitz (2007), J. Mol. Biol. 371, 1047-1059]: the RNA-binding domain of r-protein P0 (L10), the C-terminal domain of L11 and helices 43 and 44 of the 23 S rRNA. Here, the 2.4 Å resolution electron-density map of the Hma 50S ribosomal subunit was revisited and approximately two-thirds of the P0 protein, residues 1-58 of the N-terminal domains of two P1 protein molecules, residues 130-156 of L11, the full-length r-protein LX, nucleotides 2137-2149 and 2226-2237 of the 23S rRNA helix H76 forming the L1 stalk, nucleotides 2339-2343 of the 23S rRNA (contacting L5 protein) and loops 29-34 and 108-128 of protein L5 could be visualized. Thus, this paper provides a supplemented version of the Hma 50S ribosomal subunit model. PubMed: 23695244DOI: 10.1107/S0907444913004745 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.404 Å) |
Structure validation
Download full validation report
