4xww: Difference between revisions
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<StructureSection load='4xww' size='340' side='right'caption='[[4xww]], [[Resolution|resolution]] 1.70Å' scene=''> | <StructureSection load='4xww' size='340' side='right'caption='[[4xww]], [[Resolution|resolution]] 1.70Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4xww]] is a 4 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4xww]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Deinococcus_radiodurans Deinococcus radiodurans] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XWW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4XWW FirstGlance]. <br> | ||
</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=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=MN:MANGANESE+(II)+ION'>MN</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=4xww FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xww OCA], [https://pdbe.org/4xww PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4xww RCSB], [https://www.ebi.ac.uk/pdbsum/4xww PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4xww ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/H9CZL7_DEIRD H9CZL7_DEIRD] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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==See Also== | ==See Also== | ||
*[[Ribonuclease|Ribonuclease]] | *[[Ribonuclease 3D structures|Ribonuclease 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Deinococcus radiodurans]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Hua | [[Category: Synthetic construct]] | ||
[[Category: Lu | [[Category: Hua Y]] | ||
[[Category: Xu | [[Category: Lu M]] | ||
[[Category: Zhang | [[Category: Xu Q]] | ||
[[Category: Zhao | [[Category: Zhang H]] | ||
[[Category: Zhao Y]] | |||
Revision as of 20:55, 26 April 2023
Crystal structure of RNase J complexed with RNACrystal structure of RNase J complexed with RNA
Structural highlights
FunctionPublication Abstract from PubMedRNase J is a conserved ribonuclease that belongs to the beta-CASP family of nucleases. It possesses both endo- and exo-ribonuclease activities, which play a key role in pre-rRNA maturation and mRNA decay. Here we report high-resolution crystal structures of Deinococcus radiodurans RNase J complexed with RNA or uridine 5'-monophosphate in the presence of manganese ions. Biochemical and structural studies revealed that RNase J uses zinc ions for two-metal-ion catalysis. One residue conserved among RNase J orthologues (motif B) forms specific electrostatic interactions with the scissile phosphate of the RNA that is critical for the catalysis and product stabilization. The additional manganese ion, which is coordinated by conserved residues at the dimer interface, is critical for RNase J dimerization and exonuclease activity. The structures may also shed light on the mechanism of RNase J exo- and endonucleolytic activity switch. Structural insights into catalysis and dimerization enhanced exonuclease activity of RNase J.,Zhao Y, Lu M, Zhang H, Hu J, Zhou C, Xu Q, Ul Hussain Shah AM, Xu H, Wang L, Hua Y Nucleic Acids Res. 2015 Jun 23;43(11):5550-9. doi: 10.1093/nar/gkv444. Epub 2015 , May 4. PMID:25940620[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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