6h3z: Difference between revisions
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==Crystal structure of a C-terminal MIF4G domain in NOT1== | |||
<StructureSection load='6h3z' size='340' side='right' caption='[[6h3z]], [[Resolution|resolution]] 3.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6h3z]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6H3Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6H3Z FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=6h3z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6h3z OCA], [http://pdbe.org/6h3z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6h3z RCSB], [http://www.ebi.ac.uk/pdbsum/6h3z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6h3z ProSAT]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The CCR4-NOT complex plays a central role in the regulation of gene expression and degradation of messenger RNAs. The multisubunit complex assembles on the NOT1 protein, which acts as a 'scaffold' and is highly conserved in eukaryotes. NOT1 consists of a series of helical domains that serve as docking sites for other CCR4-NOT subunits. We describe a crystal structure of a connector domain of NOT1 from the thermophilic fungus Chaetomium thermophilum (Ct). Comparative structural analysis indicates that this domain adopts a MIF4G-like fold and we have termed it the MIF4G-C domain. Solution scattering studies indicate that the human MIF4G-C domain likely adopts a very similar fold to the Ct MIF4G-C. MIF4G domains have been described to mediate interactions with DEAD-box helicases such as DDX6. However, comparison of the interfaces of the MIF4G-C with the MIF4G domain of NOT1 that interacts with DDX6 reveals key structural differences that explain why the MIF4G-C does not bind DDX6. We further show that the human MIF4G-C does not interact stably with other subunits of the CCR4-NOT complex. The structural conservation of the MIF4G-C domain suggests that it may have an important but presently undefined role in the CCR4-NOT complex. | |||
Structural and biochemical analysis of a NOT1 MIF4G-like domain of the CCR4-NOT complex.,Raisch T, Sandmeir F, Weichenrieder O, Valkov E, Izaurralde E J Struct Biol. 2018 Oct 24. pii: S1047-8477(18)30282-X. doi:, 10.1016/j.jsb.2018.10.009. PMID:30367941<ref>PMID:30367941</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 6h3z" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Izaurralde, E]] | |||
[[Category: Raisch, T]] | |||
[[Category: Sandmeir, F]] | |||
[[Category: Valkov, E]] | |||
[[Category: Weichenrieder, O]] | |||
[[Category: Ccr4-not]] | |||
[[Category: Deadenylation]] | |||
[[Category: Gene regulation]] | |||
[[Category: Hydrolase]] | |||
[[Category: Mrna decay]] | |||
[[Category: Transcription]] | |||
Revision as of 12:21, 7 November 2018
Crystal structure of a C-terminal MIF4G domain in NOT1
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