1nbs: Difference between revisions

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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>
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<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.
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>
From MEDLINE&reg;/PubMed&reg;, 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/>
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</StructureSection>
</StructureSection>

Latest revision as of 10:55, 14 February 2024

Crystal structure of the specificity domain of Ribonuclease P RNACrystal structure of the specificity domain of Ribonuclease P RNA

Structural highlights

1nbs is a 2 chain structure with sequence from Bacillus subtilis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.15Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

See Also

1nbs, resolution 3.15Å

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