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2hbj

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Revision as of 08:09, 18 October 2017

Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain

Structural highlights

2hbj is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2hbk, 2hbl, 2hbm
Gene:	RRP6 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[RRP6_YEAST] Nuclear-specific catalytic component of the RNA exosome complex which has 3'->5' exoribonuclease activity and participates in a multitude of cellular RNA processing and degradation events. In the nucleus, the RNA exosome complex is involved in proper maturation of stable RNA species such as rRNA, snRNA and snoRNA, in the elimination of RNA processing by-products and non-coding 'pervasive' transcripts, such as antisense RNA species and cryptic unstable transcripts (CUTs), and of mRNAs with processing defects, thereby limiting or excluding their export to the cytoplasm. The catalytic inactive RNA exosome core complex of 9 subunits (Exo-9) is proposed to play a pivotal role in the binding and presentation of RNA for ribonucleolysis, and to serve as a scaffold for the association with catalytic subunits and accessory proteins or complexes. RRP6 has 3'-5' exonuclease activity which is not modulated upon association with Exo-9 suggesting that the complex inner RNA-binding path is not used to access its active site.^[1] ^[2] ^[3] ^[4]

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 PubMed

The multisubunit eukaryotic exosome is an essential RNA processing and degradation machine. In its nuclear form, the exosome associates with the auxiliary factor Rrp6p, which participates in both RNA processing and degradation reactions. The crystal structure of Saccharomyces cerevisiae Rrp6p displays a conserved RNase D core with a flanking HRDC (helicase and RNase D C-terminal) domain in an unusual conformation shown to be important for the processing function of the enzyme. Complexes with AMP and UMP, the products of the RNA degradation process, reveal how the protein specifically recognizes ribonucleotides and their bases. Finally, in vivo mutational studies show the importance of the domain contacts for the processing function of Rrp6p and highlight fundamental differences between the protein and its prokaryotic RNase D counterparts.

Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain.,Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11898-903. Epub 2006 Aug 1. PMID:16882719^[5]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Briggs MW, Burkard KT, Butler JS. Rrp6p, the yeast homologue of the human PM-Scl 100-kDa autoantigen, is essential for efficient 5.8 S rRNA 3' end formation. J Biol Chem. 1998 May 22;273(21):13255-63. PMID:9582370
↑ Allmang C, Petfalski E, Podtelejnikov A, Mann M, Tollervey D, Mitchell P. The yeast exosome and human PM-Scl are related complexes of 3' --> 5' exonucleases. Genes Dev. 1999 Aug 15;13(16):2148-58. PMID:10465791
↑ Burkard KT, Butler JS. A nuclear 3'-5' exonuclease involved in mRNA degradation interacts with Poly(A) polymerase and the hnRNA protein Npl3p. Mol Cell Biol. 2000 Jan;20(2):604-16. PMID:10611239
↑ Hieronymus H, Yu MC, Silver PA. Genome-wide mRNA surveillance is coupled to mRNA export. Genes Dev. 2004 Nov 1;18(21):2652-62. Epub 2004 Oct 15. PMID:15489286 doi:http://dx.doi.org/gad.1241204
↑ Midtgaard SF, Assenholt J, Jonstrup AT, Van LB, Jensen TH, Brodersen DE. Structure of the nuclear exosome component Rrp6p reveals an interplay between the active site and the HRDC domain. Proc Natl Acad Sci U S A. 2006 Aug 8;103(32):11898-903. Epub 2006 Aug 1. PMID:16882719

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hbj"

@@ Line 1: / Line 1: @@
 ==Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain==
 <StructureSection load='2hbj' size='340' side='right' caption='[[2hbj]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2hbk|2hbk]], [[2hbl|2hbl]], [[2hbm|2hbm]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RRP6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
-<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=2hbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hbj OCA], [http://pdbe.org/2hbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hbj RCSB], [http://www.ebi.ac.uk/pdbsum/2hbj PDBsum]</span></td></tr>
+<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=2hbj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hbj OCA], [http://pdbe.org/2hbj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hbj RCSB], [http://www.ebi.ac.uk/pdbsum/2hbj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hbj ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 30: / Line 31: @@
 ==See Also==
-*[[Exonuclease|Exonuclease]]
 *[[Exosome|Exosome]]
 == References ==

2hbj

From Proteopedia

Revision as of 08:09, 18 October 2017

Structure of the yeast nuclear exosome component, Rrp6p, reveals an interplay between the active site and the HRDC domain

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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