1nbs
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbs OCA], [https://pdbe.org/1nbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbs RCSB], [https://www.ebi.ac.uk/pdbsum/1nbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbs ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbs OCA], [https://pdbe.org/1nbs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nbs RCSB], [https://www.ebi.ac.uk/pdbsum/1nbs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbs ProSAT]</span></td></tr> | ||
</table> | </table> | ||
- | <div style="background-color:#fffaf0;"> | ||
- | == Publication Abstract from PubMed == | ||
- | 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. | ||
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- | Crystal structure of the specificity domain of ribonuclease P.,Krasilnikov AS, Yang X, Pan T, Mondragon A Nature. 2003 Feb 13;421(6924):760-4. PMID:12610630<ref>PMID:12610630</ref> | ||
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- | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
- | </div> | ||
- | <div class="pdbe-citations 1nbs" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
- | == References == | ||
- | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> |
Current revision
Crystal structure of the specificity domain of Ribonuclease P RNA
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