1N88
NMR structure of the ribosomal protein L23 from Thermus thermophilus.
Summary for 1N88
| Entry DOI | 10.2210/pdb1n88/pdb |
| Descriptor | Ribosomal protein L23 (1 entity in total) |
| Functional Keywords | nmr spectroscopy, protein structure, l23, ribosome, translation |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 10759.81 |
| Authors | Ohman, A.,Rak, A.,Dontsova, M.,Garber, M.B.,Hard, T. (deposition date: 2002-11-20, release date: 2003-06-10, Last modification date: 2024-05-29) |
| Primary citation | Ohman, A.,Rak, A.,Dontsova, M.,Garber, M.B.,Hard, T. NMR structure of the ribosomal protein L23 from Thermus thermophilus. J.Biomol.NMR, 26:131-137, 2003 Cited by PubMed Abstract: The ribosomal protein L23 is a component of the large ribosomal subunit in which it is located close to the peptide exit tunnel. In this position L23 plays a central role both for protein secretion and folding. We have determined the solution structure of L23 from Thermus thermophilus. Uncomplexed L23 consists of a well-ordered part, with four anti-parallel beta-strands and three alpha-helices connected as beta-alpha-beta-alpha-beta-beta-alpha, and a large and flexible loop inserted between the third and fourth beta-strand. The observed topology is distantly related to previously known structures, primarily within the area of RNA biochemistry. A comparison with RNA-complexed crystal structures of L23 from T. thermophilus, Deinococcus radiodurans and Haloarcula marismourtui, shows that the conformation of the well-ordered part is very similar in the uncomplexed and complexed states. However, the flexible loop found in the uncomplexed solution structure forms a rigid extended structure in the complexed crystal structures as it interacts with rRNA and becomes part of the exit tunnel wall. Structural characteristics of importance for the interaction with rRNA and with the ribosomal protein L29, as well as the functional role of L23, are discussed. PubMed: 12766408DOI: 10.1023/A:1023502307069 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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