1AD2
RIBOSOMAL PROTEIN L1 MUTANT WITH SERINE 179 REPLACED BY CYSTEINE
Summary for 1AD2
| Entry DOI | 10.2210/pdb1ad2/pdb |
| Descriptor | RIBOSOMAL PROTEIN L1, SULFATE ION, MERCURY (II) ION, ... (5 entities in total) |
| Functional Keywords | ribosomal protein, rna binding, protein synthesis, mutant |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 25359.52 |
| Authors | Unge, J.,Al-Karadaghi, S.,Liljas, A.,Jonsson, B.-H.,Eliseikina, I.,Ossina, N.,Nevskaya, N.,Fomenkova, N.,Garber, M.,Nikonov, S. (deposition date: 1997-02-20, release date: 1997-05-15, Last modification date: 2024-02-07) |
| Primary citation | Unge, J.,Al-Karadaghi, S.,Liljas, A.,Jonsson, B.H.,Eliseikina, I.,Ossina, N.,Nevskaya, N.,Fomenkova, N.,Garber, M.,Nikonov, S. A mutant form of the ribosomal protein L1 reveals conformational flexibility. FEBS Lett., 411:53-59, 1997 Cited by PubMed Abstract: The crystal structure of the mutant S179C of the ribosomal protein L1 from Thermus thermophilus has been determined at 1.9 A resolution. The mutant molecule displays a small but significant opening of the cavity between the two domains. The domain movement seems to be facilitated by the flexibility of at least two conserved glycines. These glycines may be necessary for the larger conformational change needed for an induced fit mechanism upon binding RNA. The domain movement makes a disulfide bridge possible between the incorporated cysteines in two monomers of the mutant L1. PubMed: 9247141DOI: 10.1016/S0014-5793(97)00611-X PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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