6l5o: Difference between revisions

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New page: '''Unreleased structure''' The entry 6l5o is ON HOLD Authors: Description: Category: Unreleased Structures
 
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'''Unreleased structure'''


The entry 6l5o is ON HOLD
==Crystal structure of human DEAD-box RNA helicase DDX21 at post-hydrolysis state==
<StructureSection load='6l5o' size='340' side='right'caption='[[6l5o]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6l5o]] is a 1 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=6L5O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6L5O FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=6l5o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6l5o OCA], [https://pdbe.org/6l5o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6l5o RCSB], [https://www.ebi.ac.uk/pdbsum/6l5o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6l5o ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DDX21_HUMAN DDX21_HUMAN] RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Involved in rRNA processing (PubMed:14559904, PubMed:18180292).<ref>PMID:11823437</ref> <ref>PMID:14559904</ref> <ref>PMID:18180292</ref> <ref>PMID:25260534</ref> <ref>PMID:25470060</ref> <ref>PMID:25477391</ref> <ref>PMID:9461305</ref>


Authors:  
==See Also==
 
*[[Helicase 3D structures|Helicase 3D structures]]
Description:  
== References ==
[[Category: Unreleased Structures]]
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Chen ZJ]]
[[Category: Hu XJ]]
[[Category: Li JX]]
[[Category: Zhou Z]]

Latest revision as of 13:45, 27 March 2024

Crystal structure of human DEAD-box RNA helicase DDX21 at post-hydrolysis stateCrystal structure of human DEAD-box RNA helicase DDX21 at post-hydrolysis state

Structural highlights

6l5o is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.8Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DDX21_HUMAN RNA helicase that acts as a sensor of the transcriptional status of both RNA polymerase (Pol) I and II: promotes ribosomal RNA (rRNA) processing and transcription from polymerase II (Pol II) (PubMed:25470060). Binds various RNAs, such as rRNAs, snoRNAs, 7SK and, at lower extent, mRNAs (PubMed:25470060). In the nucleolus, localizes to rDNA locus, where it directly binds rRNAs and snoRNAs, and promotes rRNA transcription, processing and modification. Required for rRNA 2'-O-methylation, possibly by promoting the recruitment of late-acting snoRNAs SNORD56 and SNORD58 with pre-ribosomal complexes (PubMed:25470060, PubMed:25477391). In the nucleoplasm, binds 7SK RNA and is recruited to the promoters of Pol II-transcribed genes: acts by facilitating the release of P-TEFb from inhibitory 7SK snRNP in a manner that is dependent on its helicase activity, thereby promoting transcription of its target genes (PubMed:25470060). Functions as cofactor for JUN-activated transcription: required for phosphorylation of JUN at 'Ser-77' (PubMed:11823437, PubMed:25260534). Can unwind double-stranded RNA (helicase) and can fold or introduce a secondary structure to a single-stranded RNA (foldase) (PubMed:9461305). Involved in rRNA processing (PubMed:14559904, PubMed:18180292).[1] [2] [3] [4] [5] [6] [7]

See Also

References

  1. ↑ Westermarck J, Weiss C, Saffrich R, Kast J, Musti AM, Wessely M, Ansorge W, Seraphin B, Wilm M, Valdez BC, Bohmann D. The DEXD/H-box RNA helicase RHII/Gu is a co-factor for c-Jun-activated transcription. EMBO J. 2002 Feb 1;21(3):451-60. PMID:11823437
  2. ↑ Henning D, So RB, Jin R, Lau LF, Valdez BC. Silencing of RNA helicase II/Gualpha inhibits mammalian ribosomal RNA production. J Biol Chem. 2003 Dec 26;278(52):52307-14. Epub 2003 Oct 13. PMID:14559904 doi:http://dx.doi.org/10.1074/jbc.M310846200
  3. ↑ Holmstrom TH, Mialon A, Kallio M, Nymalm Y, Mannermaa L, Holm T, Johansson H, Black E, Gillespie D, Salminen TA, Langel U, Valdez BC, Westermarck J. c-Jun supports ribosomal RNA processing and nucleolar localization of RNA helicase DDX21. J Biol Chem. 2008 Mar 14;283(11):7046-53. doi: 10.1074/jbc.M709613200. Epub 2008 , Jan 7. PMID:18180292 doi:http://dx.doi.org/10.1074/jbc.M709613200
  4. ↑ Zhang Y, Baysac KC, Yee LF, Saporita AJ, Weber JD. Elevated DDX21 regulates c-Jun activity and rRNA processing in human breast cancers. Breast Cancer Res. 2014 Sep 28;16(5):449. doi: 10.1186/s13058-014-0449-z. PMID:25260534 doi:http://dx.doi.org/10.1186/s13058-014-0449-z
  5. ↑ Calo E, Flynn RA, Martin L, Spitale RC, Chang HY, Wysocka J. RNA helicase DDX21 coordinates transcription and ribosomal RNA processing. Nature. 2015 Feb 12;518(7538):249-53. doi: 10.1038/nature13923. Epub 2014 Nov 24. PMID:25470060 doi:http://dx.doi.org/10.1038/nature13923
  6. ↑ Sloan KE, Leisegang MS, Doebele C, Ramirez AS, Simm S, Safferthal C, Kretschmer J, Schorge T, Markoutsa S, Haag S, Karas M, Ebersberger I, Schleiff E, Watkins NJ, Bohnsack MT. The association of late-acting snoRNPs with human pre-ribosomal complexes requires the RNA helicase DDX21. Nucleic Acids Res. 2015 Jan;43(1):553-64. doi: 10.1093/nar/gku1291. Epub 2014 Dec, 4. PMID:25477391 doi:http://dx.doi.org/10.1093/nar/gku1291
  7. ↑ Valdez BC, Henning D, Perumal K, Busch H. RNA-unwinding and RNA-folding activities of RNA helicase II/Gu--two activities in separate domains of the same protein. Eur J Biochem. 1997 Dec 15;250(3):800-7. PMID:9461305

6l5o, resolution 1.80Å

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