3rc3: Difference between revisions

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==See Also==
*[[Helicase|Helicase]]
== References ==
== References ==
<references/>
<references/>

Revision as of 12:24, 8 November 2017

Human Mitochondrial Helicase Suv3Human Mitochondrial Helicase Suv3

Structural highlights

3rc3 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
NonStd Res:
Gene:SUPV3L1, SUV3 (HUMAN)
Activity:RNA helicase, with EC number 3.6.4.13
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SUV3_HUMAN] Major helicase player in mitochondrial RNA metabolism. Component of the mitochondrial degradosome (mtEXO) complex, that degrades 3' overhang double-stranded RNA with a 3'-to-5' directionality in an ATP-dependent manner. ATPase and ATP-dependent multisubstrate helicase, able to unwind double-stranded (ds) DNA and RNA, and RNA/DNA heteroduplexes in the 5'-to-3' direction. Plays a role in the RNA surveillance system in mitochondria; regulates the stability of mature mRNAs, the removal of aberrantly formed mRNAs and the rapid degradation of non coding processing intermediates. Also implicated in recombination and chromatin maintenance pathways. May protect cells from apoptosis. Associates with mitochondrial DNA.[1] [2] [3] [4] [5] [6] [7]

Publication Abstract from PubMed

Suv3 is a helicase that is involved in efficient turnover and surveillance of RNA in eukaryotes. In vitro studies show that human Suv3 (hSuv3) in complex with human polynucleotide phosphorylase has RNA degradosome activity. The enzyme is mainly localized in mitochondria, but small fractions are found in cell nuclei. Here, two X-ray crystallographic structures of human Suv3 in complex with AMPPNP, a nonhydrolysable analog of ATP, and with a short five-nucleotide strand of RNA are presented at resolutions of 2.08 and 2.9 A, respectively. The structure of the enzyme is very similar in the two complexes and consists of four domains. Two RecA-like domains form the tandem typical of all helicases from the SF2 superfamily which together with the C-terminal all-helical domain makes a ring structure through which the nucleotide strand threads. The mostly helical N-terminal domain is positioned externally with respect to the core of the enzyme. Most of the typical helicase motifs are present in hSuv3, but the protein shows certain unique characteristics, suggesting that Suv3 enzymes may constitute a separate subfamily of helicases.

Human Suv3 protein reveals unique features among SF2 helicases.,Jedrzejczak R, Wang J, Dauter M, Szczesny RJ, Stepien PP, Dauter Z Acta Crystallogr D Biol Crystallogr. 2011 Nov;67(Pt 11):988-96. Epub 2011 Oct 19. PMID:22101826[8]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. ↑ Minczuk M, Piwowarski J, Papworth MA, Awiszus K, Schalinski S, Dziembowski A, Dmochowska A, Bartnik E, Tokatlidis K, Stepien PP, Borowski P. Localisation of the human hSuv3p helicase in the mitochondrial matrix and its preferential unwinding of dsDNA. Nucleic Acids Res. 2002 Dec 1;30(23):5074-86. PMID:12466530
  2. ↑ Shu Z, Vijayakumar S, Chen CF, Chen PL, Lee WH. Purified human SUV3p exhibits multiple-substrate unwinding activity upon conformational change. Biochemistry. 2004 Apr 27;43(16):4781-90. PMID:15096047 doi:http://dx.doi.org/10.1021/bi0356449
  3. ↑ Szczesny RJ, Obriot H, Paczkowska A, Jedrzejczak R, Dmochowska A, Bartnik E, Formstecher P, Polakowska R, Stepien PP. Down-regulation of human RNA/DNA helicase SUV3 induces apoptosis by a caspase- and AIF-dependent pathway. Biol Cell. 2007 Jun;99(6):323-32. PMID:17352692 doi:http://dx.doi.org/BC20060108
  4. ↑ Pereira M, Mason P, Szczesny RJ, Maddukuri L, Dziwura S, Jedrzejczak R, Paul E, Wojcik A, Dybczynska L, Tudek B, Bartnik E, Klysik J, Bohr VA, Stepien PP. Interaction of human SUV3 RNA/DNA helicase with BLM helicase; loss of the SUV3 gene results in mouse embryonic lethality. Mech Ageing Dev. 2007 Nov-Dec;128(11-12):609-17. Epub 2007 Sep 14. PMID:17961633 doi:http://dx.doi.org/10.1016/j.mad.2007.09.001
  5. ↑ Khidr L, Wu G, Davila A, Procaccio V, Wallace D, Lee WH. Role of SUV3 helicase in maintaining mitochondrial homeostasis in human cells. J Biol Chem. 2008 Oct 3;283(40):27064-73. doi: 10.1074/jbc.M802991200. Epub 2008 , Aug 4. PMID:18678873 doi:http://dx.doi.org/10.1074/jbc.M802991200
  6. ↑ Wang DD, Shu Z, Lieser SA, Chen PL, Lee WH. Human mitochondrial SUV3 and polynucleotide phosphorylase form a 330-kDa heteropentamer to cooperatively degrade double-stranded RNA with a 3'-to-5' directionality. J Biol Chem. 2009 Jul 31;284(31):20812-21. Epub 2009 Jun 9. PMID:19509288 doi:M109.009605
  7. ↑ Szczesny RJ, Borowski LS, Brzezniak LK, Dmochowska A, Gewartowski K, Bartnik E, Stepien PP. Human mitochondrial RNA turnover caught in flagranti: involvement of hSuv3p helicase in RNA surveillance. Nucleic Acids Res. 2010 Jan;38(1):279-98. Epub 2009 Oct 28. PMID:19864255 doi:http://dx.doi.org/gkp903
  8. ↑ Jedrzejczak R, Wang J, Dauter M, Szczesny RJ, Stepien PP, Dauter Z. Human Suv3 protein reveals unique features among SF2 helicases. Acta Crystallogr D Biol Crystallogr. 2011 Nov;67(Pt 11):988-96. Epub 2011 Oct 19. PMID:22101826 doi:10.1107/S0907444911040248

3rc3, resolution 2.08Å

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