3zq4
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Unusual, dual endo- and exo-nuclease activity in the degradosome explained by crystal structure analysis of RNase J1== | |
| + | <StructureSection load='3zq4' size='340' side='right'caption='[[3zq4]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3zq4]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis_subsp._subtilis_str._168 Bacillus subtilis subsp. subtilis str. 168]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3ZQ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3ZQ4 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]] 3Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=3zq4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3zq4 OCA], [https://pdbe.org/3zq4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3zq4 RCSB], [https://www.ebi.ac.uk/pdbsum/3zq4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3zq4 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/RNJ1_BACSU RNJ1_BACSU] An RNase that has endonuclease and 5'-3' exonuclease activity, playing a role in both rRNA and mRNA stability and degradation. Endonuclease activity can cleave within 4 nucleotides of the 5'-end of a triphosphorylated RNA. Endonuclease digestion by the RNase J1/J2 complex occurs at a different site and in some cases more efficiently than J1 or J2 alone. The exonuclease activity of the J1/J2 complex is highly processive on substrates longer than 5 nucleotides, on shorter substrates is distributive. Preferentially cleaves ssRNA, possibly in AU-rich regions. The 5'-exonuclease activity acts on 5'-hydroxyl and 5'-monophosphate but not 5'-triphosphate ends; it can digest through stem-loop structures if they are not too stable. Required for maturation of 16S rRNA. Acts preferentially on 16S rRNA precursors after association of the 30S and 50S ribosomal subunits. Plays a role in the secondary pathway of 23S rRNA 5' end maturation. Probably also participates in processing of pre-scRNA (the precursor of the signal recognition particle RNA).<ref>PMID:15831787</ref> <ref>PMID:17229210</ref> <ref>PMID:17512403</ref> <ref>PMID:17576666</ref> <ref>PMID:18204464</ref> <ref>PMID:18445592</ref> <ref>PMID:18713320</ref> <ref>PMID:19880604</ref> <ref>PMID:20025672</ref> <ref>PMID:21893286</ref> <ref>PMID:22014150</ref> <ref>PMID:22412379</ref> <ref>PMID:23504012</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | RNase J is an essential enzyme in Bacillus subtilis with unusual dual endonuclease and 5'-to-3' exonuclease activities that play an important role in the maturation and degradation of mRNA. RNase J is also a component of the recently identified "degradosome" of B. subtilis. We report the crystal structure of RNase J1 from B. subtilis to 3.0 A resolution, analysis of which reveals it to be in an open conformation suitable for binding substrate RNA. RNase J is a member of the beta-CASP family of zinc-dependent metallo-beta-lactamases. We have exploited this similarity in constructing a model for an RNase J1:RNA complex. Analysis of this model reveals candidate-stacking interactions with conserved aromatic side chains, providing a molecular basis for the observed enzyme activity. Comparisons of the B. subtilis RNase J structure with related enzymes reveal key differences that provide insights into conformational changes during catalysis and the role of the C-terminal domain. | ||
| - | + | Unusual, Dual Endo- and Exonuclease Activity in the Degradosome Explained by Crystal Structure Analysis of RNase J1.,Newman JA, Hewitt L, Rodrigues C, Solovyova A, Harwood CR, Lewis RJ Structure. 2011 Sep 7;19(9):1241-51. PMID:21893285<ref>PMID:21893285</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 3zq4" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Bacillus subtilis subsp. subtilis str. 168]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Harwood CR]] | ||
| + | [[Category: Hewitt L]] | ||
| + | [[Category: Lewis RJ]] | ||
| + | [[Category: Newman JA]] | ||
| + | [[Category: Rodrigues C]] | ||
| + | [[Category: Solovyova A]] | ||
Current revision
Unusual, dual endo- and exo-nuclease activity in the degradosome explained by crystal structure analysis of RNase J1
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