4wfc: Difference between revisions

Line 1:

'''~~Unreleased~~ structure'''

==Structure of the Rrp6-Rrp47 interaction==

== Structural highlights ==

<table><tr><td colspan='2'>[[4wfc]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WFC FirstGlance]. <br>

</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>

<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=4wfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wfc RCSB], [http://www.ebi.ac.uk/pdbsum/4wfc PDBsum]</span></td></tr>

</table>

== Publication Abstract from PubMed ==

The exosome is a conserved multi-subunit ribonuclease complex that functions in 3' end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and functionally interacts with the Rrp6 exoribonuclease and its associated cofactor Rrp47, the helicase Mtr4 and Mpp6. Here, we show that binding of Mtr4 to Exo-10 in vitro is dependent upon both Rrp6 and Rrp47, whereas Mpp6 binds directly and independently of other cofactors. Crystallographic analyses reveal that the N-terminal domains of Rrp6 and Rrp47 form a highly intertwined structural unit. Rrp6 and Rrp47 synergize to create a composite and conserved surface groove that binds the N-terminus of Mtr4. Mutation of conserved residues within Rrp6 and Mtr4 at the structural interface disrupts their interaction and inhibits growth of strains expressing a C-terminal GFP fusion of Mtr4. These studies provide detailed structural insight into the interaction between the Rrp6-Rrp47 complex and Mtr4, revealing an important link between Mtr4 and the core exosome.

The ~~entry 4wfc is ON HOLD until Paper Publication~~

The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.,Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E EMBO J. 2014 Oct 15. pii: e201488757. PMID:25319414<ref>PMID:25319414</ref>

~~Authors: Schuch~~, B., Conti, E.

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

</div>

~~Description~~:

== References ==

__TOC__

</StructureSection>

[[Category: Conti, E.]]

[[Category: Schuch, B.]]

[[Category: Hydrolase]]

[[Category: Nuclear exosome]]

[[Category: Rna degradation]]

[[Category: Rna processing]]

[[Category: Rrp6-rrp47 complex]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+==Structure of the Rrp6-Rrp47 interaction==
+<StructureSection load='4wfc' size='340' side='right' caption='[[4wfc]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4wfc]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4WFC OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4WFC FirstGlance]. <br>
+</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>
+<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=4wfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4wfc OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4wfc RCSB], [http://www.ebi.ac.uk/pdbsum/4wfc PDBsum]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The exosome is a conserved multi-subunit ribonuclease complex that functions in 3' end processing, turnover and surveillance of nuclear and cytoplasmic RNAs. In the yeast nucleus, the 10-subunit core complex of the exosome (Exo-10) physically and functionally interacts with the Rrp6 exoribonuclease and its associated cofactor Rrp47, the helicase Mtr4 and Mpp6. Here, we show that binding of Mtr4 to Exo-10 in vitro is dependent upon both Rrp6 and Rrp47, whereas Mpp6 binds directly and independently of other cofactors. Crystallographic analyses reveal that the N-terminal domains of Rrp6 and Rrp47 form a highly intertwined structural unit. Rrp6 and Rrp47 synergize to create a composite and conserved surface groove that binds the N-terminus of Mtr4. Mutation of conserved residues within Rrp6 and Mtr4 at the structural interface disrupts their interaction and inhibits growth of strains expressing a C-terminal GFP fusion of Mtr4. These studies provide detailed structural insight into the interaction between the Rrp6-Rrp47 complex and Mtr4, revealing an important link between Mtr4 and the core exosome.
-The entry 4wfc is ON HOLD  until Paper Publication
+The exosome-binding factors Rrp6 and Rrp47 form a composite surface for recruiting the Mtr4 helicase.,Schuch B, Feigenbutz M, Makino DL, Falk S, Basquin C, Mitchell P, Conti E EMBO J. 2014 Oct 15. pii: e201488757. PMID:25319414<ref>PMID:25319414</ref>
-Authors: Schuch, B., Conti, E.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description:
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Conti, E.]]
+[[Category: Schuch, B.]]
+[[Category: Hydrolase]]
+[[Category: Nuclear exosome]]
+[[Category: Rna degradation]]
+[[Category: Rna processing]]
+[[Category: Rrp6-rrp47 complex]]