1DD4
Crystal structure of ribosomal protein l12 from thermotoga maritim
Summary for 1DD4
| Entry DOI | 10.2210/pdb1dd4/pdb |
| Related | 1DD3 |
| Descriptor | 50S RIBOSOMAL PROTEIN L7/L12, HEXATANTALUM DODECABROMIDE, ... (4 entities in total) |
| Functional Keywords | dimer formation, flexibility, hinge region, four-helix-bundle, five-helix- bundle, alpha-beta structure, helical hairpin, domains, ribosome |
| Biological source | Thermotoga maritima More |
| Total number of polymer chains | 4 |
| Total formula weight | 39562.02 |
| Authors | Wahl, M.C.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R. (deposition date: 1999-11-08, release date: 2000-11-13, Last modification date: 2024-05-22) |
| Primary citation | Wahl, M.C.,Bourenkov, G.P.,Bartunik, H.D.,Huber, R. Flexibility, conformational diversity and two dimerization modes in complexes of ribosomal protein L12. Embo J., 19:174-186, 2000 Cited by PubMed Abstract: Protein L12, the only multicopy component of the ribosome, is presumed to be involved in the binding of translation factors, stimulating factor-dependent GTP hydrolysis. Crystal structures of L12 from Thermotogamaritima have been solved in two space groups by the multiple anomalous dispersion method and refined at 2.4 and 2.0 A resolution. In both crystal forms, an asymmetric unit comprises two full-length L12 molecules and two N-terminal L12 fragments that are associated in a specific, hetero-tetrameric complex with one non-crystallographic 2-fold axis. The two full-length proteins form a tight, symmetric, parallel dimer, mainly through their N-terminal domains. Each monomer of this central dimer additionally associates in a different way with an N-terminal L12 fragment. Both dimerization modes are unlike models proposed previously and suggest that similar complexes may occur in vivo and in situ. The structures also display different L12 monomer conformations, in accord with the suggested dynamic role of the protein in the ribosomal translocation process. The structures have been submitted to the Protein Databank (http://www.rcsb.org/pdb) under accession numbers 1DD3 and 1DD4. PubMed: 10637222DOI: 10.1093/emboj/19.2.174 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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