6h3z

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'''Unreleased structure'''
 
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The entry 6h3z is ON HOLD until Paper Publication
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==Crystal structure of a C-terminal MIF4G domain in NOT1==
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<StructureSection load='6h3z' size='340' side='right' caption='[[6h3z]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</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>
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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=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>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6h3z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Izaurralde, E]]
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[[Category: Raisch, T]]
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[[Category: Sandmeir, F]]
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[[Category: Valkov, E]]
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[[Category: Weichenrieder, O]]
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[[Category: Ccr4-not]]
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[[Category: Deadenylation]]
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[[Category: Gene regulation]]
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[[Category: Hydrolase]]
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[[Category: Mrna decay]]
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[[Category: Transcription]]

Revision as of 12:21, 7 November 2018

Crystal structure of a C-terminal MIF4G domain in NOT1

6h3z, resolution 3.00Å

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