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2i7x

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Revision as of 08:24, 18 October 2017

Structure of Yeast CPSF-100 (Ydh1p)

Structural highlights

2i7x is a 1 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	2i7t, 2i7v
Gene:	CFT2, YDH1 (ATCC 18824)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CFT2_YEAST] RNA-binding component of the cleavage and polyadenylation factor (CPF) complex, which plays a key role in polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with cleavage factors including the CFIA complex and NAB4/CFIB. May be involved in poly(A)-site recognition. May be involved in the association of the CPF, CPFIA and RNA polymerase II complexes.^[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

Most eukaryotic messenger RNA precursors (pre-mRNAs) undergo extensive maturational processing, including cleavage and polyadenylation at the 3'-end. Despite the characterization of many proteins that are required for the cleavage reaction, the identity of the endonuclease is not known. Recent analyses indicated that the 73-kDa subunit of cleavage and polyadenylation specificity factor (CPSF-73) might be the endonuclease for this and related reactions, although no direct data confirmed this. Here we report the crystal structures of human CPSF-73 at 2.1 A resolution, complexed with zinc ions and a sulphate that might mimic the phosphate group of the substrate, and the related yeast protein CPSF-100 (Ydh1) at 2.5 A resolution. Both CPSF-73 and CPSF-100 contain two domains, a metallo-beta-lactamase domain and a novel beta-CASP (named for metallo-beta-lactamase, CPSF, Artemis, Snm1, Pso2) domain. The active site of CPSF-73, with two zinc ions, is located at the interface of the two domains. Purified recombinant CPSF-73 possesses RNA endonuclease activity, and mutations that disrupt zinc binding in the active site abolish this activity. Our studies provide the first direct experimental evidence that CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.

Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease.,Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L Nature. 2006 Dec 14;444(7121):953-6. Epub 2006 Nov 26. PMID:17128255^[3]

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

References

↑ Dichtl B, Keller W. Recognition of polyadenylation sites in yeast pre-mRNAs by cleavage and polyadenylation factor. EMBO J. 2001 Jun 15;20(12):3197-209. PMID:11406596 doi:http://dx.doi.org/10.1093/emboj/20.12.3197
↑ Kyburz A, Sadowski M, Dichtl B, Keller W. The role of the yeast cleavage and polyadenylation factor subunit Ydh1p/Cft2p in pre-mRNA 3'-end formation. Nucleic Acids Res. 2003 Jul 15;31(14):3936-45. PMID:12853609
↑ Mandel CR, Kaneko S, Zhang H, Gebauer D, Vethantham V, Manley JL, Tong L. Polyadenylation factor CPSF-73 is the pre-mRNA 3'-end-processing endonuclease. Nature. 2006 Dec 14;444(7121):953-6. Epub 2006 Nov 26. PMID:17128255 doi:10.1038/nature05363

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/2i7x"

@@ Line 1: / Line 1: @@
 ==Structure of Yeast CPSF-100 (Ydh1p)==
 <StructureSection load='2i7x' size='340' side='right' caption='[[2i7x]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2i7t|2i7t]], [[2i7v|2i7v]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CFT2, YDH1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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=2i7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i7x OCA], [http://pdbe.org/2i7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i7x RCSB], [http://www.ebi.ac.uk/pdbsum/2i7x 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=2i7x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i7x OCA], [http://pdbe.org/2i7x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2i7x RCSB], [http://www.ebi.ac.uk/pdbsum/2i7x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2i7x ProSAT]</span></td></tr>
 </table>
 == Function ==

2i7x

From Proteopedia

Revision as of 08:24, 18 October 2017

Structure of Yeast CPSF-100 (Ydh1p)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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