2p51

From Proteopedia

(Difference between revisions)

Revision as of 09:18, 18 October 2017

Crystal structure of the S. pombe Pop2p deadenylation subunit

Structural highlights

2p51 is a 1 chain structure with sequence from Cbs 356. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Gene:	SPCC18.06c (caf1 homologue) (CBS 356)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CAF1_SCHPO] Acts as the catalytic component of the CCR4-NOT core complex, which in the nucleus seems to be a general transcription factor, and in the cytoplasm the major mRNA deadenylase involved in mRNA turnover. In vivo and in vitro, caf1 has 3'-exoribonuclease activity with a preference for poly(A) RNAs.^[1] ^[2]

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

Deadenylation is the first and probably also rate-limiting step of controlled mRNA decay in eukaryotes and therefore central for the overall rate of gene expression. In yeast, the process is maintained by the mega-Dalton Ccr4-Not complex, of which both the Ccr4p and Pop2p subunits are 3'-5' exonucleases potentially responsible for the deadenylation reaction. Here, we present the crystal structure of the Pop2p subunit from Schizosaccharomyces pombe determined to 1.4 A resolution and show that the enzyme is a competent ribonuclease with a tunable specificity towards poly-A. In contrast to S. cerevisiae Pop2p, the S. pombe enzyme contains a fully conserved DEDDh active site, and the high resolution allows for a detailed analysis of its configuration, including divalent metal ion binding. Functional data further indicates that the identity of the ions in the active site can modulate both activity and specificity of the enzyme, and finally structural superposition of single nucleotides and poly-A oligonucleotides provide insight into the catalytic cycle of the protein.

The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme.,Jonstrup AT, Andersen KR, Van LB, Brodersen DE Nucleic Acids Res. 2007;35(9):3153-64. Epub 2007 Apr 22. PMID:17452359^[3]

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

References

↑ Jonstrup AT, Andersen KR, Van LB, Brodersen DE. The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme. Nucleic Acids Res. 2007;35(9):3153-64. Epub 2007 Apr 22. PMID:17452359 doi:http://dx.doi.org/10.1093/nar/gkm178
↑ Andersen KR, Jonstrup AT, Van LB, Brodersen DE. The activity and selectivity of fission yeast Pop2p are affected by a high affinity for Zn2+ and Mn2+ in the active site. RNA. 2009 May;15(5):850-61. Epub 2009 Mar 23. PMID:19307292 doi:10.1261/rna.1489409
↑ Jonstrup AT, Andersen KR, Van LB, Brodersen DE. The 1.4-A crystal structure of the S. pombe Pop2p deadenylase subunit unveils the configuration of an active enzyme. Nucleic Acids Res. 2007;35(9):3153-64. Epub 2007 Apr 22. PMID:17452359 doi:http://dx.doi.org/10.1093/nar/gkm178

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2p51"

@@ Line 1: / Line 1: @@
 ==Crystal structure of the S. pombe Pop2p deadenylation subunit==
 <StructureSection load='2p51' size='340' side='right' caption='[[2p51]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SPCC18.06c (caf1 homologue) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4896 CBS 356])</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=2p51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p51 OCA], [http://pdbe.org/2p51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p51 RCSB], [http://www.ebi.ac.uk/pdbsum/2p51 PDBsum]</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=2p51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p51 OCA], [http://pdbe.org/2p51 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p51 RCSB], [http://www.ebi.ac.uk/pdbsum/2p51 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p51 ProSAT]</span></td></tr>
 </table>
 == Function ==

2p51

From Proteopedia

Revision as of 09:18, 18 October 2017

Crystal structure of the S. pombe Pop2p deadenylation subunit

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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