7z4z: Difference between revisions
New page: '''Unreleased structure''' The entry 7z4z is ON HOLD Authors: Description: Category: Unreleased Structures |
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The | ==Human NEXT dimer - focused reconstruction of the dimerization module== | ||
<StructureSection load='7z4z' size='340' side='right'caption='[[7z4z]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7z4z]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7Z4Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7Z4Z FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4Å</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=7z4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7z4z OCA], [https://pdbe.org/7z4z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7z4z RCSB], [https://www.ebi.ac.uk/pdbsum/7z4z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7z4z ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/ZCHC8_HUMAN ZCHC8_HUMAN] May be involved in pre-mRNA splicing. | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
In mammalian cells, spurious transcription results in a vast repertoire of unproductive non-coding RNAs, whose deleterious accumulation is prevented by rapid decay. The nuclear exosome targeting (NEXT) complex plays a central role in directing non-functional transcripts to exosome-mediated degradation, but the structural and molecular mechanisms remain enigmatic. Here, we elucidated the architecture of the human NEXT complex, showing that it exists as a dimer of MTR4-ZCCHC8-RBM7 heterotrimers. Dimerization preconfigures the major MTR4-binding region of ZCCHC8 and arranges the two MTR4 helicases opposite to each other, with each protomer able to function on many types of RNAs. In the inactive state of the complex, the 3' end of an RNA substrate is enclosed in the MTR4 helicase channel by a ZCCHC8 C-terminal gatekeeping domain. The architecture of a NEXT-exosome assembly points to the molecular and regulatory mechanisms with which the NEXT complex guides RNA substrates to the exosome. | |||
Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome.,Gerlach P, Garland W, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Jensen TH, Conti E Mol Cell. 2022 Jul 7;82(13):2505-2518.e7. doi: 10.1016/j.molcel.2022.04.011. Epub , 2022 Jun 9. PMID:35688157<ref>PMID:35688157</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 7z4z" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Exosome 3D structures|Exosome 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Basquin J]] | |||
[[Category: Bonneau F]] | |||
[[Category: Conti E]] | |||
[[Category: Gerlach P]] | |||
[[Category: Lingaraju M]] | |||
[[Category: Salerno-Kochan A]] | |||
Latest revision as of 15:41, 17 July 2024
Human NEXT dimer - focused reconstruction of the dimerization moduleHuman NEXT dimer - focused reconstruction of the dimerization module
Structural highlights
FunctionZCHC8_HUMAN May be involved in pre-mRNA splicing. Publication Abstract from PubMedIn mammalian cells, spurious transcription results in a vast repertoire of unproductive non-coding RNAs, whose deleterious accumulation is prevented by rapid decay. The nuclear exosome targeting (NEXT) complex plays a central role in directing non-functional transcripts to exosome-mediated degradation, but the structural and molecular mechanisms remain enigmatic. Here, we elucidated the architecture of the human NEXT complex, showing that it exists as a dimer of MTR4-ZCCHC8-RBM7 heterotrimers. Dimerization preconfigures the major MTR4-binding region of ZCCHC8 and arranges the two MTR4 helicases opposite to each other, with each protomer able to function on many types of RNAs. In the inactive state of the complex, the 3' end of an RNA substrate is enclosed in the MTR4 helicase channel by a ZCCHC8 C-terminal gatekeeping domain. The architecture of a NEXT-exosome assembly points to the molecular and regulatory mechanisms with which the NEXT complex guides RNA substrates to the exosome. Structure and regulation of the nuclear exosome targeting complex guides RNA substrates to the exosome.,Gerlach P, Garland W, Lingaraju M, Salerno-Kochan A, Bonneau F, Basquin J, Jensen TH, Conti E Mol Cell. 2022 Jul 7;82(13):2505-2518.e7. doi: 10.1016/j.molcel.2022.04.011. Epub , 2022 Jun 9. PMID:35688157[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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