4ro1
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4ro1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RO1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4ro1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RO1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RO1 FirstGlance]. <br> | ||
| - | </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=4ro1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ro1 OCA], [https://pdbe.org/4ro1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ro1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ro1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ro1 ProSAT]</span></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]] 2.803Å</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=4ro1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ro1 OCA], [https://pdbe.org/4ro1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ro1 RCSB], [https://www.ebi.ac.uk/pdbsum/4ro1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ro1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/DI3L2_SCHPO DI3L2_SCHPO] 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'.[HAMAP-Rule:MF_03045]<ref>PMID:23503588</ref> | [https://www.uniprot.org/uniprot/DI3L2_SCHPO DI3L2_SCHPO] 3'-5'-exoribonuclease that specifically recognizes RNAs polyuridylated at their 3' end and mediates their degradation. Component of an exosome-independent RNA degradation pathway that mediates degradation of cytoplasmic mRNAs that have been deadenylated and subsequently uridylated at their 3'.[HAMAP-Rule:MF_03045]<ref>PMID:23503588</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | After deadenylation and decapping, cytoplasmic mRNA can be digested in two opposite directions: in the 5'-3' direction by Xrn1 or in the 3'-5' direction by the exosome complex. Recently, a novel 3'-5' RNA-decay pathway involving Dis3l2 has been described that differs from degradation by Xrn1 and the exosome. The product of the Schizosaccharomyces pombe gene SPAC2C4.07c was identified as a homologue of human Dis3l2. In this work, the 2.8 A resolution X-ray crystal structure of S. pombe Dis3l2 (SpDis3l2) is reported, the conformation of which is obviously different from that in the homologous mouse Dis3l2-RNA complex. Fluorescence polarization assay experiments showed that RNB and S1 are the primary RNA-binding domains and that the CSDs (CSD1 and CSD2) play an indispensable role in the RNA-binding process of SpDis3l2. Taking the structure comparison and mutagenic experiments together, it can be inferred that the RNA-recognition pattern of SpDis3l2 resembles that of its mouse homologue rather than that of the Escherichia coli RNase II-RNA complex. Furthermore, a drastic conformation change could occur following the binding of the RNA substrate to SpDis3l2. | ||
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| - | Structural analysis of Dis3l2, an exosome-independent exonuclease from Schizosaccharomyces pombe.,Lv H, Zhu Y, Qiu Y, Niu L, Teng M, Li X Acta Crystallogr D Biol Crystallogr. 2015 Jun;71(Pt 6):1284-94. doi:, 10.1107/S1399004715005805. Epub 2015 May 14. PMID:26057668<ref>PMID:26057668</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4ro1" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
An 3'-5'-exoribonuclease that specifically recognizes RNAs.
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