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3ngo

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Revision as of 14:12, 25 December 2014

Crystal structure of the human CNOT6L nuclease domain in complex with poly(A) DNA

Structural highlights

3ngo is a 2 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:
Related:	3ngn, 3ngq
Gene:	CNOT6L, CCR4B (Homo sapiens)
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[CNO6L_HUMAN] Plays a role in the deadenylation of mRNAs in the cytoplasm. Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. May be involved in the deadenylation-dependent degradation of mRNAs through the 3'-UTR AU-rich element-mediated mechanism. Involved in deadenylation-dependent degradation of CDKN1B mRNA.^[1]

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

CCR4, an evolutionarily conserved member of the CCR4-NOT complex, is the main cytoplasmic deadenylase. It contains a C-terminal nuclease domain with homology to the endonuclease-exonuclease-phosphatase (EEP) family of enzymes. We have determined the high-resolution three-dimensional structure of the nuclease domain of CNOT6L, a human homologue of CCR4, by X-ray crystallography using the single-wavelength anomalous dispersion method. This first structure of a deadenylase belonging to the EEP family adopts a complete alpha/beta sandwich fold typical of hydrolases with highly conserved active site residues similar to APE1. The active site of CNOT6L should recognize the RNA substrate through its negatively charged surface. In vitro deadenylase assays confirm the critical active site residues and show that the nuclease domain of CNOT6L exhibits full Mg(2+)-dependent deadenylase activity with strict poly(A) RNA substrate specificity. To understand the structural basis for poly(A) RNA substrate binding, crystal structures of the CNOT6L nuclease domain have also been determined in complex with AMP and poly(A) DNA. The resulting structures suggest a molecular deadenylase mechanism involving a pentacovalent phosphate transition.

Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity.,Wang H, Morita M, Yang X, Suzuki T, Yang W, Wang J, Ito K, Wang Q, Zhao C, Bartlam M, Yamamoto T, Rao Z EMBO J. 2010 Aug 4;29(15):2566-76. Epub 2010 Jul 13. PMID:20628353^[2]

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

References

↑ Morita M, Suzuki T, Nakamura T, Yokoyama K, Miyasaka T, Yamamoto T. Depletion of mammalian CCR4b deadenylase triggers elevation of the p27Kip1 mRNA level and impairs cell growth. Mol Cell Biol. 2007 Jul;27(13):4980-90. Epub 2007 Apr 23. PMID:17452450 doi:MCB.02304-06
↑ Wang H, Morita M, Yang X, Suzuki T, Yang W, Wang J, Ito K, Wang Q, Zhao C, Bartlam M, Yamamoto T, Rao Z. Crystal structure of the human CNOT6L nuclease domain reveals strict poly(A) substrate specificity. EMBO J. 2010 Aug 4;29(15):2566-76. Epub 2010 Jul 13. PMID:20628353 doi:10.1038/emboj.2010.152

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/3ngo"

@@ 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=3ngo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ngo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ngo RCSB], [http://www.ebi.ac.uk/pdbsum/3ngo PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/CNO6L_HUMAN CNO6L_HUMAN]] Plays a role in the deadenylation of mRNAs in the cytoplasm. Has 3'-5' poly(A) exoribonuclease activity for synthetic poly(A) RNA substrate. May be involved in the deadenylation-dependent degradation of mRNAs through the 3'-UTR AU-rich element-mediated mechanism. Involved in deadenylation-dependent degradation of CDKN1B mRNA.<ref>PMID:17452450</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 26: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+==See Also==
+*[[Ribonuclease|Ribonuclease]]
+*[[Temp|Temp]]
 == References ==
 <references/>

3ngo

From Proteopedia

Revision as of 14:12, 25 December 2014

Crystal structure of the human CNOT6L nuclease domain in complex with poly(A) DNA

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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