4buj

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<StructureSection load='4buj' size='340' side='right'caption='[[4buj]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
<StructureSection load='4buj' size='340' side='right'caption='[[4buj]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4buj]] is a 8 chain structure with sequence from [http://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4BUJ FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4buj]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BUJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BUJ 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=SO4:SULFATE+ION'>SO4</scene></td></tr>
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</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>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></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=4buj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buj OCA], [https://pdbe.org/4buj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4buj RCSB], [https://www.ebi.ac.uk/pdbsum/4buj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4buj ProSAT]</span></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </span></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=4buj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4buj OCA], [http://pdbe.org/4buj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4buj RCSB], [http://www.ebi.ac.uk/pdbsum/4buj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4buj ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/SKI2_YEAST SKI2_YEAST]] RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.<ref>PMID:8321235</ref> <ref>PMID:363683</ref> <ref>PMID:6371496</ref> <ref>PMID:7739552</ref> <ref>PMID:7739557</ref> <ref>PMID:9482746</ref> <ref>PMID:10611222</ref> <ref>PMID:10744028</ref> <ref>PMID:10922069</ref> <ref>PMID:11532933</ref> <ref>PMID:11720286</ref> <ref>PMID:12769863</ref> <ref>PMID:14671320</ref> [[http://www.uniprot.org/uniprot/SKI8_YEAST SKI8_YEAST]] Involved in double-strand break (DSB) formation during meiotic recombination through stabilization of SPO11 association with meiotic chromosome and helping SPO11 to recruit other DSB proteins like REC102 and REC104 to meiotic chromosomes. Also component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for controlling the propagation of M double-stranded RNA (dsRNA) and thus for preventing virus-induced cytopathology.<ref>PMID:6371496</ref> <ref>PMID:3029964</ref> <ref>PMID:7739557</ref> <ref>PMID:9258672</ref> <ref>PMID:9482746</ref> <ref>PMID:10744028</ref> <ref>PMID:11532933</ref> <ref>PMID:11720286</ref> <ref>PMID:14671320</ref> <ref>PMID:15044957</ref> <ref>PMID:14992724</ref> <ref>PMID:16816949</ref> [[http://www.uniprot.org/uniprot/SKI3_YEAST SKI3_YEAST]] Component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.<ref>PMID:363683</ref> <ref>PMID:6371496</ref> <ref>PMID:7739552</ref> <ref>PMID:7739557</ref> <ref>PMID:9482746</ref> <ref>PMID:10744028</ref> <ref>PMID:11532933</ref> <ref>PMID:11720286</ref> <ref>PMID:14671320</ref>
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[[https://www.uniprot.org/uniprot/SKI2_YEAST SKI2_YEAST]] RNA helicase component of the SKI complex involved in 3'-mRNA degradation pathway. Represses dsRNA virus propagation by specifically blocking translation of viral mRNAs, perhaps recognizing the absence of CAP or poly(A). Essential for cell growth only in the presence of M1 replicon.<ref>PMID:8321235</ref> <ref>PMID:363683</ref> <ref>PMID:6371496</ref> <ref>PMID:7739552</ref> <ref>PMID:7739557</ref> <ref>PMID:9482746</ref> <ref>PMID:10611222</ref> <ref>PMID:10744028</ref> <ref>PMID:10922069</ref> <ref>PMID:11532933</ref> <ref>PMID:11720286</ref> <ref>PMID:12769863</ref> <ref>PMID:14671320</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Ski complex is a conserved multiprotein assembly required for the cytoplasmic functions of the exosome, including RNA turnover, surveillance, and interference. Ski2, Ski3, and Ski8 assemble in a tetramer with 1:1:2 stoichiometry. The crystal structure of an S. cerevisiae 370 kDa core complex shows that Ski3 forms an array of 33 TPR motifs organized in N-terminal and C-terminal arms. The C-terminal arm of Ski3 and the two Ski8 subunits position the helicase core of Ski2 centrally within the complex, enhancing RNA binding. The Ski3 N-terminal arm and the Ski2 insertion domain allosterically modulate the ATPase and helicase activities of the complex. Biochemical data suggest that the Ski complex can thread RNAs directly to the exosome, coupling the helicase and the exoribonuclease through a continuous RNA channel. Finally, we identify a Ski8-binding motif common to Ski3 and Spo11, rationalizing the moonlighting properties of Ski8 in mRNA decay and meiosis.
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The yeast ski complex: crystal structure and RNA channeling to the exosome complex.,Halbach F, Reichelt P, Rode M, Conti E Cell. 2013 Aug 15;154(4):814-26. doi: 10.1016/j.cell.2013.07.017. PMID:23953113<ref>PMID:23953113</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 4buj" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Baker's yeast]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: RNA helicase]]
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Conti, E]]
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[[Category: Conti E]]
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[[Category: Halbach, F]]
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[[Category: Halbach F]]
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[[Category: Reichelt, P]]
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[[Category: Reichelt P]]
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[[Category: Rode, M]]
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[[Category: Rode M]]
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[[Category: Dexh box helicase]]
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[[Category: Hydrolase]]
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[[Category: Protein complex]]
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[[Category: Rna degradation]]
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[[Category: Tpr]]
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Revision as of 17:08, 7 September 2022

Crystal structure of the S. cerevisiae Ski2-3-8 complex

PDB ID 4buj

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