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3l7z
From Proteopedia
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| - | {{Seed}} | ||
| - | [[Image:3l7z.jpg|left|200px]] | ||
| - | < | + | ==Crystal structure of the S. solfataricus archaeal exosome== |
| - | + | <StructureSection load='3l7z' size='340' side='right'caption='[[3l7z]], [[Resolution|resolution]] 2.41Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[3l7z]] is a 9 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_35091 Atcc 35091]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L7Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3L7Z FirstGlance]. <br> | |
| - | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | |
| - | - | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C20_023, Rrp41/42/4, SSO0732 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091]), SSO0735 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091]), C20_026, SSO0736 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2287 ATCC 35091])</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=3l7z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l7z OCA], [https://pdbe.org/3l7z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3l7z RCSB], [https://www.ebi.ac.uk/pdbsum/3l7z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3l7z ProSAT]</span></td></tr> | |
| + | </table> | ||
| + | == 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/ECR1_SULSO ECR1_SULSO]] Probably involved in degradation of a variety of RNA species; could act a RNA-binding component of the exosome (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 == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/l7/3l7z_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=3l7z ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | BACKGROUND: The exosome complex is an essential RNA 3'-end processing and degradation machinery. In archaeal organisms, the exosome consists of a catalytic ring and an RNA-binding ring, both of which were previously reported to assume three-fold symmetry. METHODOLOGY/PRINCIPAL FINDINGS: Here we report an asymmetric 2.9 A Sulfolobus solfataricus archaeal exosome structure in which the three-fold symmetry is broken due to combined rigid body and thermal motions mainly within the RNA-binding ring. Since increased conformational flexibility was also observed in the RNA-binding ring of the related bacterial PNPase, we speculate that this may reflect an evolutionarily conserved mechanism to accommodate diverse RNA substrates for degradation. CONCLUSION/SIGNIFICANCE: This study clearly shows the dynamic structures within the RNA-binding domains, which provides additional insights on mechanism of asymmetric RNA binding and processing. | ||
| - | + | Crystal structure of the S. solfataricus archaeal exosome reveals conformational flexibility in the RNA-binding ring.,Lu C, Ding F, Ke A PLoS One. 2010 Jan 15;5(1):e8739. PMID:20090900<ref>PMID:20090900</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 3l7z" style="background-color:#fffaf0;"></div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | == | + | [[Category: Atcc 35091]] |
| - | + | [[Category: Large Structures]] | |
| - | + | [[Category: Ding, F]] | |
| - | == | + | [[Category: Ke, A]] |
| - | < | + | [[Category: Lu, C]] |
| - | [[Category: | + | |
| - | [[Category: Ding, F | + | |
| - | [[Category: Ke, A | + | |
| - | [[Category: Lu, C | + | |
[[Category: Asymmetry]] | [[Category: Asymmetry]] | ||
[[Category: Conformation flexibility]] | [[Category: Conformation flexibility]] | ||
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[[Category: Rna processing]] | [[Category: Rna processing]] | ||
[[Category: Thermal motion]] | [[Category: Thermal motion]] | ||
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jun 23 08:49:59 2010'' | ||
Current revision
Crystal structure of the S. solfataricus archaeal exosome
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