1nbs: Difference between revisions
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<StructureSection load='1nbs' size='340' side='right'caption='[[1nbs]], [[Resolution|resolution]] 3.15Å' scene=''> | <StructureSection load='1nbs' size='340' side='right'caption='[[1nbs]], [[Resolution|resolution]] 3.15Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<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 [https://proteopedia.org/fgij/fg.htm?mol=1NBS FirstGlance]. <br> | <table><tr><td colspan='2'>[[1nbs]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1NBS FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.15Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PB:LEAD+(II)+ION'>PB</scene></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> | <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> | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Bacillus subtilis]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Krasilnikov | [[Category: Krasilnikov AS]] | ||
[[Category: Mondragon | [[Category: Mondragon A]] | ||
[[Category: Pan | [[Category: Pan T]] | ||
[[Category: Yang | [[Category: Yang X]] | ||
Revision as of 14:24, 2 August 2023
Crystal structure of the specificity domain of Ribonuclease P RNACrystal structure of the specificity domain of Ribonuclease P RNA
Structural highlights
Publication Abstract from PubMedRNase 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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