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3t3o

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

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@@ Line 3: / Line 3: @@
 <StructureSection load='3t3o' size='340' side='right'caption='[[3t3o]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3t3o]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3T3O FirstGlance]. <br>
+<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>
-</td></tr><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=ZN:ZINC+ION'>ZN</scene></td></tr>
+</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>
-<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>
+<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>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3bk1|3bk1]], [[3bk2|3bk2]], [[3t3n|3t3n]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ttc0775, TT_C0775 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=262724 THET2])</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=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>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[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>
-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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3t3o" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 24: / Line 15: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Thet2]]
+[[Category: Thermus thermophilus HB27]]
-[[Category: Condon, C]]
+[[Category: Condon C]]
-[[Category: Dorleans, A]]
+[[Category: Dorleans A]]
-[[Category: Gilet, L]]
+[[Category: Gilet L]]
-[[Category: Piton, J]]
+[[Category: Li de la Sierra-Gallay I]]
-[[Category: Putzer, H]]
+[[Category: Piton J]]
-[[Category: Sierra-Gallay, I Li de la]]
+[[Category: Putzer H]]
-[[Category: Zig, L]]
+[[Category: Zig L]]
-[[Category: 5'-3' exoribonuclease]]
-[[Category: Endoribonuclease]]
-[[Category: Hydrolase]]
-[[Category: Hydrolase-rna complex]]
-[[Category: Metal dependent hydrolase]]
-[[Category: Metallo-beta-lactamase]]
-[[Category: Protein-rna complex]]
-[[Category: Rna]]
-[[Category: Rnase j]]

3t3o

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

Structural highlights

Function

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