6ro1: Difference between revisions

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'''Unreleased structure'''


The entry 6ro1 is ON HOLD until Paper Publication
==X-ray crystal structure of the MTR4 NVL complex==
 
<StructureSection load='6ro1' size='340' side='right'caption='[[6ro1]], [[Resolution|resolution]] 3.07&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6ro1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RO1 FirstGlance]. <br>
Description:  
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
[[Category: Unreleased Structures]]
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/RNA_helicase RNA helicase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.4.13 3.6.4.13] </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=6ro1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ro1 OCA], [http://pdbe.org/6ro1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ro1 RCSB], [http://www.ebi.ac.uk/pdbsum/6ro1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ro1 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MTREX_HUMAN MTREX_HUMAN]] Component of exosome targeting complexes. Subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that directs a subset of non-coding short-lived RNAs for exosomal degradation. Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters (PubMed:27871484). May be involved in pre-mRNA splicing. Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA.<ref>PMID:17412707</ref> <ref>PMID:27871484</ref> [[http://www.uniprot.org/uniprot/NVL_HUMAN NVL_HUMAN]] Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT (PubMed:22226966). Involved in both early and late stages of the pre-rRNA processing pathways (PubMed:26166824). Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucleolus (PubMed:15469983, PubMed:16782053, PubMed:29107693, PubMed:26456651). Catalyzes the release of specific assembly factors, such as WDR74, from pre-60S ribosomal particles through the ATPase activity (PubMed:29107693, PubMed:26456651, PubMed:28416111).<ref>PMID:15469983</ref> <ref>PMID:16782053</ref> <ref>PMID:22226966</ref> <ref>PMID:26166824</ref> <ref>PMID:26456651</ref> <ref>PMID:28416111</ref> <ref>PMID:29107693</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: RNA helicase]]
[[Category: Basquin, J]]
[[Category: Conti, E]]
[[Category: Falk, S]]
[[Category: Langer, L M]]
[[Category: Lingaraju, M]]
[[Category: Complex]]
[[Category: Dexh helicase]]
[[Category: Rna binding protein]]

Revision as of 09:11, 3 July 2019

X-ray crystal structure of the MTR4 NVL complexX-ray crystal structure of the MTR4 NVL complex

Structural highlights

6ro1 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:RNA helicase, with EC number 3.6.4.13
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MTREX_HUMAN] Component of exosome targeting complexes. Subunit of the trimeric nuclear exosome targeting (NEXT) complex, a complex that directs a subset of non-coding short-lived RNAs for exosomal degradation. Subunit of the trimeric poly(A) tail exosome targeting (PAXT) complex, a complex that directs a subset of long and polyadenylated poly(A) RNAs for exosomal degradation. The RNA exosome is fundamental for the degradation of RNA in eukaryotic nuclei. Substrate targeting is facilitated by its cofactor MTREX, which links to RNA-binding protein adapters (PubMed:27871484). May be involved in pre-mRNA splicing. Associated with the RNA exosome complex and involved in the 3'-processing of the 7S pre-RNA to the mature 5.8S rRNA.[1] [2] [NVL_HUMAN] Participates in the assembly of the telomerase holoenzyme and effecting of telomerase activity via its interaction with TERT (PubMed:22226966). Involved in both early and late stages of the pre-rRNA processing pathways (PubMed:26166824). Spatiotemporally regulates 60S ribosomal subunit biogenesis in the nucleolus (PubMed:15469983, PubMed:16782053, PubMed:29107693, PubMed:26456651). Catalyzes the release of specific assembly factors, such as WDR74, from pre-60S ribosomal particles through the ATPase activity (PubMed:29107693, PubMed:26456651, PubMed:28416111).[3] [4] [5] [6] [7] [8] [9]

References

  1. ↑ Schilders G, van Dijk E, Pruijn GJ. C1D and hMtr4p associate with the human exosome subunit PM/Scl-100 and are involved in pre-rRNA processing. Nucleic Acids Res. 2007;35(8):2564-72. Epub 2007 Apr 4. PMID:17412707 doi:http://dx.doi.org/10.1093/nar/gkm082
  2. ↑ Meola N, Domanski M, Karadoulama E, Chen Y, Gentil C, Pultz D, Vitting-Seerup K, Lykke-Andersen S, Andersen JS, Sandelin A, Jensen TH. Identification of a Nuclear Exosome Decay Pathway for Processed Transcripts. Mol Cell. 2016 Nov 3;64(3):520-533. doi: 10.1016/j.molcel.2016.09.025. Epub 2016 , Oct 27. PMID:27871484 doi:http://dx.doi.org/10.1016/j.molcel.2016.09.025
  3. ↑ Nagahama M, Hara Y, Seki A, Yamazoe T, Kawate Y, Shinohara T, Hatsuzawa K, Tani K, Tagaya M. NVL2 is a nucleolar AAA-ATPase that interacts with ribosomal protein L5 through its nucleolar localization sequence. Mol Biol Cell. 2004 Dec;15(12):5712-23. doi: 10.1091/mbc.e04-08-0692. Epub 2004, Oct 6. PMID:15469983 doi:http://dx.doi.org/10.1091/mbc.e04-08-0692
  4. ↑ Nagahama M, Yamazoe T, Hara Y, Tani K, Tsuji A, Tagaya M. The AAA-ATPase NVL2 is a component of pre-ribosomal particles that interacts with the DExD/H-box RNA helicase DOB1. Biochem Biophys Res Commun. 2006 Aug 4;346(3):1075-82. doi:, 10.1016/j.bbrc.2006.06.017. Epub 2006 Jun 12. PMID:16782053 doi:http://dx.doi.org/10.1016/j.bbrc.2006.06.017
  5. ↑ Her J, Chung IK. The AAA-ATPase NVL2 is a telomerase component essential for holoenzyme assembly. Biochem Biophys Res Commun. 2012 Jan 20;417(3):1086-92. doi:, 10.1016/j.bbrc.2011.12.101. Epub 2011 Dec 27. PMID:22226966 doi:http://dx.doi.org/10.1016/j.bbrc.2011.12.101
  6. ↑ Yoshikatsu Y, Ishida Y, Sudo H, Yuasa K, Tsuji A, Nagahama M. NVL2, a nucleolar AAA-ATPase, is associated with the nuclear exosome and is involved in pre-rRNA processing. Biochem Biophys Res Commun. 2015 Aug 28;464(3):780-6. doi:, 10.1016/j.bbrc.2015.07.032. Epub 2015 Jul 10. PMID:26166824 doi:http://dx.doi.org/10.1016/j.bbrc.2015.07.032
  7. ↑ Hiraishi N, Ishida Y, Nagahama M. AAA-ATPase NVL2 acts on MTR4-exosome complex to dissociate the nucleolar protein WDR74. Biochem Biophys Res Commun. 2015 Nov 20;467(3):534-40. doi:, 10.1016/j.bbrc.2015.09.160. Epub 2015 Oct 8. PMID:26456651 doi:http://dx.doi.org/10.1016/j.bbrc.2015.09.160
  8. ↑ Lo YH, Romes EM, Pillon MC, Sobhany M, Stanley RE. Structural Analysis Reveals Features of Ribosome Assembly Factor Nsa1/WDR74 Important for Localization and Interaction with Rix7/NVL2. Structure. 2017 May 2;25(5):762-772.e4. doi: 10.1016/j.str.2017.03.008. Epub 2017, Apr 13. PMID:28416111 doi:http://dx.doi.org/10.1016/j.str.2017.03.008
  9. ↑ Hiraishi N, Ishida YI, Sudo H, Nagahama M. WDR74 participates in an early cleavage of the pre-rRNA processing pathway in cooperation with the nucleolar AAA-ATPase NVL2. Biochem Biophys Res Commun. 2018 Jan 1;495(1):116-123. doi:, 10.1016/j.bbrc.2017.10.148. Epub 2017 Oct 28. PMID:29107693 doi:http://dx.doi.org/10.1016/j.bbrc.2017.10.148

6ro1, resolution 3.07Å

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