3ctr

From Proteopedia

(Difference between revisions)

Revision as of 13:47, 25 December 2014

Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP

Structural highlights

3ctr 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.
Ligands:
Gene:	PARN, DAN (Homo sapiens)
Activity:	Poly(A)-specific ribonuclease, with EC number 3.1.13.4
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PARN_HUMAN] 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization.^[1] ^[2] ^[3] ^[4] ^[5]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Poly(A)-specific ribonuclease (PARN) is a processive 3'-exoribonuclease involved in the decay of eukaryotic mRNAs. Interestingly, PARN interacts not only with the 3' end of the mRNA but also with its 5' end as PARN contains an RRM domain that specifically binds both the poly(A) tail and the 7-methylguanosine (m(7)G) cap. The interaction of PARN with the 5' cap of mRNAs stimulates the deadenylation activity and enhances the processivity of this reaction. We have determined the crystal structure of the PARN-RRM domain with a bound m(7)G triphosphate nucleotide, revealing a novel binding mode for the m(7)G cap. The structure of the m(7)G binding pocket is located outside of the canonical RNA-binding surface of the RRM domain and differs significantly from that of other m(7)G-cap-binding proteins. The crystal structure also shows a remarkable conformational flexibility of the RRM domain, leading to a perfect exchange of two alpha-helices with an adjacent protein molecule in the crystal lattice.

Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m(7)G-cap-binding mode.,Monecke T, Schell S, Dickmanns A, Ficner R J Mol Biol. 2008 Oct 17;382(4):827-34. Epub 2008 Jul 31. PMID:18694759^[6]

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

References

↑ Korner CG, Wormington M, Muckenthaler M, Schneider S, Dehlin E, Wahle E. The deadenylating nuclease (DAN) is involved in poly(A) tail removal during the meiotic maturation of Xenopus oocytes. EMBO J. 1998 Sep 15;17(18):5427-37. PMID:9736620 doi:http://dx.doi.org/10.1093/emboj/17.18.5427
↑ Gao M, Fritz DT, Ford LP, Wilusz J. Interaction between a poly(A)-specific ribonuclease and the 5' cap influences mRNA deadenylation rates in vitro. Mol Cell. 2000 Mar;5(3):479-88. PMID:10882133
↑ Martinez J, Ren YG, Nilsson P, Ehrenberg M, Virtanen A. The mRNA cap structure stimulates rate of poly(A) removal and amplifies processivity of degradation. J Biol Chem. 2001 Jul 27;276(30):27923-9. Epub 2001 May 18. PMID:11359775 doi:http://dx.doi.org/10.1074/jbc.M102270200
↑ Lai WS, Kennington EA, Blackshear PJ. Tristetraprolin and its family members can promote the cell-free deadenylation of AU-rich element-containing mRNAs by poly(A) ribonuclease. Mol Cell Biol. 2003 Jun;23(11):3798-812. PMID:12748283
↑ Gherzi R, Lee KY, Briata P, Wegmuller D, Moroni C, Karin M, Chen CY. A KH domain RNA binding protein, KSRP, promotes ARE-directed mRNA turnover by recruiting the degradation machinery. Mol Cell. 2004 Jun 4;14(5):571-83. PMID:15175153 doi:http://dx.doi.org/10.1016/j.molcel.2004.05.002
↑ Monecke T, Schell S, Dickmanns A, Ficner R. Crystal structure of the RRM domain of poly(A)-specific ribonuclease reveals a novel m(7)G-cap-binding mode. J Mol Biol. 2008 Oct 17;382(4):827-34. Epub 2008 Jul 31. PMID:18694759 doi:10.1016/j.jmb.2008.07.073

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ctr"

@@ Line 8: / Line 8: @@
 <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=3ctr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ctr OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ctr RCSB], [http://www.ebi.ac.uk/pdbsum/3ctr PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PARN_HUMAN PARN_HUMAN]] 3'-exoribonuclease that has a preference for poly(A) tails of mRNAs, thereby efficiently degrading poly(A) tails. Exonucleolytic degradation of the poly(A) tail is often the first step in the decay of eukaryotic mRNAs and is also used to silence certain maternal mRNAs translationally during oocyte maturation and early embryonic development. Interacts with both the 3'-end poly(A) tail and the 5'-end cap structure during degradation, the interaction with the cap structure being required for an efficient degradation of poly(A) tails. Involved in nonsense-mediated mRNA decay, a critical process of selective degradation of mRNAs that contain premature stop codons. Also involved in degradation of inherently unstable mRNAs that contain AU-rich elements (AREs) in their 3'-UTR, possibly via its interaction with KHSRP. Probably mediates the removal of poly(A) tails of AREs mRNAs, which constitutes the first step of destabilization.<ref>PMID:9736620</ref> <ref>PMID:10882133</ref> <ref>PMID:11359775</ref> <ref>PMID:12748283</ref> <ref>PMID:15175153</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 29: / Line 31: @@
 ==See Also==
 *[[Ribonuclease|Ribonuclease]]
+*[[Temp|Temp]]
+*[[User:Jaime.Prilusky/Test/tree|User:Jaime.Prilusky/Test/tree]]
 == References ==
 <references/>
@@ Line 34: / Line 38: @@
 </StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Dickmanns, A.]]
+[[Category: Dickmanns, A]]
-[[Category: Ficner, R.]]
+[[Category: Ficner, R]]
-[[Category: Monecke, T.]]
+[[Category: Monecke, T]]
-[[Category: Schell, S.]]
+[[Category: Schell, S]]
 [[Category: Exonuclease]]
 [[Category: Hydrolase]]

3ctr

From Proteopedia

Revision as of 13:47, 25 December 2014

Crystal structure of the RRM-domain of the poly(A)-specific ribonuclease PARN bound to m7GTP

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox