3t3o

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==Molecular basis for the recognition and cleavage of RNA (CUGG) by the bifunctional 5'-3' exo/endoribonuclease RNase J==
==Molecular basis for the recognition and cleavage of RNA (CUGG) by the bifunctional 5'-3' exo/endoribonuclease RNase J==
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<StructureSection load='3t3o' size='340' side='right' caption='[[3t3o]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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<StructureSection load='3t3o' size='340' side='right'caption='[[3t3o]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[3t3o]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Thet2 Thet2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3T3O FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3t3o]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermus_thermophilus_HB27 Thermus thermophilus HB27]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3T3O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3T3O FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OMC:O2-METHYLYCYTIDINE-5-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=OMC:O2-METHYLYCYTIDINE-5-MONOPHOSPHATE'>OMC</scene>, <scene name='pdbligand=OMG:O2-METHYLGUANOSINE-5-MONOPHOSPHATE'>OMG</scene>, <scene name='pdbligand=OMU:O2-METHYLURIDINE+5-MONOPHOSPHATE'>OMU</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bk1|3bk1]], [[3bk2|3bk2]], [[3t3n|3t3n]]</td></tr>
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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=3t3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3o OCA], [https://pdbe.org/3t3o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3t3o RCSB], [https://www.ebi.ac.uk/pdbsum/3t3o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3o ProSAT]</span></td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttc0775, TT_C0775 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</td></tr>
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<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=3t3o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3t3o OCA], [http://pdbe.org/3t3o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3t3o RCSB], [http://www.ebi.ac.uk/pdbsum/3t3o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3t3o ProSAT]</span></td></tr>
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</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/RNJ_THET2 RNJ_THET2] An RNase that has endonuclease and possibly 5'-3' exonuclease activity. Probably involved in maturation of rRNA and in some organisms also mRNA maturation and/or decay.<ref>PMID:18204464</ref>
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RNase J is a key member of the beta-CASP family of metallo-beta-lactamases involved in the maturation and turnover of RNAs in prokaryotes. The B. subtilis enzyme possesses both 5'-3' exoribonucleolytic and endonucleolytic activity, an unusual property for a ribonuclease. Here, we present the crystal structure of T. thermophilus RNase J bound to a 4 nucleotide RNA. The structure reveals an RNA-binding channel that illustrates how the enzyme functions in 5'-3' exoribonucleolytic mode and how it can function as an endonuclease. A second, negatively charged tunnel leads from the active site, and is ideally located to evacuate the cleaved nucleotide in 5'-3' exonucleolytic mode. We show that B. subtilis RNase J1, which shows processive behavior on long RNAs, behaves distributively for substrates less than 5 nucleotides in length. We propose a model involving the binding of the RNA to the surface of the beta-CASP domain to explain the enzyme's processive action.
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Molecular basis for the recognition and cleavage of RNA by the bifunctional 5'-3' exo/endoribonuclease RNase J.,Dorleans A, Li de la Sierra-Gallay I, Piton J, Zig L, Gilet L, Putzer H, Condon C Structure. 2011 Sep 7;19(9):1252-61. PMID:21893286<ref>PMID:21893286</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3t3o" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Thet2]]
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[[Category: Large Structures]]
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[[Category: Condon, C]]
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[[Category: Thermus thermophilus HB27]]
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[[Category: Dorleans, A]]
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[[Category: Condon C]]
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[[Category: Gilet, L]]
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[[Category: Dorleans A]]
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[[Category: Piton, J]]
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[[Category: Gilet L]]
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[[Category: Putzer, H]]
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[[Category: Li de la Sierra-Gallay I]]
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[[Category: Sierra-Gallay, I Li de la]]
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[[Category: Piton J]]
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[[Category: Zig, L]]
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[[Category: Putzer H]]
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[[Category: 5'-3' exoribonuclease]]
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[[Category: Zig L]]
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[[Category: Endoribonuclease]]
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[[Category: Hydrolase]]
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[[Category: Hydrolase-rna complex]]
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[[Category: Metal dependent hydrolase]]
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[[Category: Metallo-beta-lactamase]]
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[[Category: Protein-rna complex]]
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[[Category: Rna]]
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[[Category: Rnase j]]
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Current revision

Molecular basis for the recognition and cleavage of RNA (CUGG) by the bifunctional 5'-3' exo/endoribonuclease RNase J

PDB ID 3t3o

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