2a2e
From Proteopedia
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| - | [[Image:2a2e.gif|left|200px]]<br /><applet load="2a2e" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="2a2e, resolution 3.85Å" /> | ||
| - | '''Crystal structure of the RNA subunit of Ribonuclease P. Bacterial A-type.'''<br /> | ||
| - | == | + | ==Crystal structure of the RNA subunit of Ribonuclease P. Bacterial A-type.== |
| + | <StructureSection load='2a2e' size='340' side='right'caption='[[2a2e]], [[Resolution|resolution]] 3.85Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2a2e]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima Thermotoga maritima]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A2E FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.85Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=OS:OSMIUM+ION'>OS</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=2a2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2e OCA], [https://pdbe.org/2a2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a2e RCSB], [https://www.ebi.ac.uk/pdbsum/2a2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2e ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Transfer RNA (tRNA) is produced as a precursor molecule that needs to be processed at its 3' and 5' ends. Ribonuclease P is the sole endonuclease responsible for processing the 5' end of tRNA by cleaving the precursor and leading to tRNA maturation. It was one of the first catalytic RNA molecules identified and consists of a single RNA component in all organisms and only one protein component in bacteria. It is a true multi-turnover ribozyme and one of only two ribozymes (the other being the ribosome) that are conserved in all kingdoms of life. Here we show the crystal structure at 3.85 A resolution of the RNA component of Thermotoga maritima ribonuclease P. The entire RNA catalytic component is revealed, as well as the arrangement of the two structural domains. The structure shows the general architecture of the RNA molecule, the inter- and intra-domain interactions, the location of the universally conserved regions, the regions involved in pre-tRNA recognition and the location of the active site. A model with bound tRNA is in agreement with all existing data and suggests the general basis for RNA-RNA recognition by this ribozyme. | Transfer RNA (tRNA) is produced as a precursor molecule that needs to be processed at its 3' and 5' ends. Ribonuclease P is the sole endonuclease responsible for processing the 5' end of tRNA by cleaving the precursor and leading to tRNA maturation. It was one of the first catalytic RNA molecules identified and consists of a single RNA component in all organisms and only one protein component in bacteria. It is a true multi-turnover ribozyme and one of only two ribozymes (the other being the ribosome) that are conserved in all kingdoms of life. Here we show the crystal structure at 3.85 A resolution of the RNA component of Thermotoga maritima ribonuclease P. The entire RNA catalytic component is revealed, as well as the arrangement of the two structural domains. The structure shows the general architecture of the RNA molecule, the inter- and intra-domain interactions, the location of the universally conserved regions, the regions involved in pre-tRNA recognition and the location of the active site. A model with bound tRNA is in agreement with all existing data and suggests the general basis for RNA-RNA recognition by this ribozyme. | ||
| - | + | Crystal structure of the RNA component of bacterial ribonuclease P.,Torres-Larios A, Swinger KK, Krasilnikov AS, Pan T, Mondragon A Nature. 2005 Sep 22;437(7058):584-7. Epub 2005 Aug 21. PMID:16113684<ref>PMID:16113684</ref> | |
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| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 2a2e" style="background-color:#fffaf0;"></div> |
| - | [[Category: Krasilnikov | + | == References == |
| - | [[Category: Mondragon | + | <references/> |
| - | [[Category: Pan | + | __TOC__ |
| - | [[Category: Swinger | + | </StructureSection> |
| - | [[Category: Torres-Larios | + | [[Category: Large Structures]] |
| - | + | [[Category: Thermotoga maritima]] | |
| - | + | [[Category: Krasilnikov AS]] | |
| - | + | [[Category: Mondragon A]] | |
| - | + | [[Category: Pan T]] | |
| - | + | [[Category: Swinger KK]] | |
| - | + | [[Category: Torres-Larios A]] | |
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Current revision
Crystal structure of the RNA subunit of Ribonuclease P. Bacterial A-type.
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