2c39: Difference between revisions
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<StructureSection load='2c39' size='340' side='right'caption='[[2c39]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='2c39' size='340' side='right'caption='[[2c39]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2c39]] is a 24 chain structure with sequence from [ | <table><tr><td colspan='2'>[[2c39]] is a 24 chain structure with sequence from [https://en.wikipedia.org/wiki/'saccharolobus_solfataricus' 'saccharolobus solfataricus']. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C39 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2C39 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2br2|2br2]], [[2c37|2c37]], [[2c38|2c38]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2br2|2br2]], [[2c37|2c37]], [[2c38|2c38]]</div></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2c39 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c39 OCA], [https://pdbe.org/2c39 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2c39 RCSB], [https://www.ebi.ac.uk/pdbsum/2c39 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2c39 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ECX2_SULSO ECX2_SULSO]] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). [[https://www.uniprot.org/uniprot/ECX1_SULSO ECX1_SULSO]] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 09:47, 1 December 2021
RNase PH core of the archaeal exosome in complex with ADPRNase PH core of the archaeal exosome in complex with ADP
Structural highlights
Function[ECX2_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). [ECX1_SULSO] Probably involved in the 3'->5' degradation of a variety of RNA species (Potential). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe exosome is a macromolecular complex that plays fundamental roles in the biogenesis and turnover of a large number of RNA species. Here we report the crystal structures of the Rrp41-Rrp42 core complex of the S. solfataricus exosome bound to short single-stranded RNAs and to ADP. The RNA binding cleft recognizes four nucleotides in a sequence-unspecific manner, mainly by electrostatic interactions with the phosphate groups. Interactions at the 2' hydroxyls of the sugars provide specificity for RNA over DNA. The structures show both the bound substrate and the cleaved product of the reaction, suggesting a catalytic mechanism for the 3'-5' phosphorolytic activity of the exosome. Structural basis of 3' end RNA recognition and exoribonucleolytic cleavage by an exosome RNase PH core.,Lorentzen E, Conti E Mol Cell. 2005 Nov 11;20(3):473-81. PMID:16285928[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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