1nbs

<StructureSection load='1nbs' size='340' side='right' caption='[[1nbs]], [[Resolution|resolution]] 3.15&Aring;' scene=''>

<table><tr><td colspan='2'>[[1nbs]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NBS OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NBS FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nxl|1nxl]]</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nbs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nbs OCA], [http://pdbe.org/1nbs PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nbs RCSB], [http://www.ebi.ac.uk/pdbsum/1nbs PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1nbs ProSAT]</span></td></tr>

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== 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>

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<div class="pdbe-citations 1nbs" style="background-color:#fffaf0;"></div>

*[[Ribonuclease|Ribonuclease]]

[[Category: Krasilnikov, A S]]

[[Category: Mondragon, A]]

[[Category: Pan, T]]

[[Category: Yang, X]]

[[Category: P rna]]

[[Category: Ribonuclease p rna]]

[[Category: S-domain]]