1NBS
Crystal structure of the specificity domain of Ribonuclease P RNA
Summary for 1NBS
| Entry DOI | 10.2210/pdb1nbs/pdb |
| Related | 1NXL |
| Descriptor | RIBONUCLEASE P RNA, MAGNESIUM ION, LEAD (II) ION (3 entities in total) |
| Functional Keywords | ribonuclease p rna, p rna, s-domain, rna |
| Biological source | Bacillus subtilis |
| Total number of polymer chains | 2 |
| Total formula weight | 105477.15 |
| Authors | Krasilnikov, A.S.,Yang, X.,Pan, T.,Mondragon, A. (deposition date: 2002-12-03, release date: 2003-02-18, Last modification date: 2024-02-14) |
| Primary citation | Krasilnikov, A.S.,Yang, X.,Pan, T.,Mondragon, A. Crystal structure of the specificity domain of Ribonuclease P Nature, 421:760-764, 2003 Cited by PubMed Abstract: RNase P is the only endonuclease responsible for processing the 5' end of transfer RNA by cleaving a precursor and leading to tRNA maturation. It contains an RNA component and a protein component and has been identified in all organisms. It was one of the first catalytic RNAs identified and the first that acts as a multiple-turnover enzyme in vivo. RNase P and the ribosome are so far the only two ribozymes known to be conserved in all kingdoms of life. The RNA component of bacterial RNase P can catalyse pre-tRNA cleavage in the absence of the RNase P protein in vitro and consists of two domains: a specificity domain and a catalytic domain. Here we report a 3.15-A resolution crystal structure of the 154-nucleotide specificity domain of Bacillus subtilis RNase P. The structure reveals the architecture of this domain, the interactions that maintain the overall fold of the molecule, a large non-helical but well-structured module that is conserved in all RNase P RNA, and the regions that are involved in interactions with the substrate. PubMed: 12610630DOI: 10.1038/nature01386 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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