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| | <StructureSection load='4c0h' size='340' side='right'caption='[[4c0h]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='4c0h' size='340' side='right'caption='[[4c0h]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4c0h]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4C0H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4c0h]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4C0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4C0H FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4c0b|4c0b]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</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=4c0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0h OCA], [http://pdbe.org/4c0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4c0h RCSB], [http://www.ebi.ac.uk/pdbsum/4c0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0h ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4c0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4c0h OCA], [https://pdbe.org/4c0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4c0h RCSB], [https://www.ebi.ac.uk/pdbsum/4c0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4c0h ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CLP1_YEAST CLP1_YEAST]] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex.<ref>PMID:11344258</ref> | + | [https://www.uniprot.org/uniprot/CLP1_YEAST CLP1_YEAST] Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex.<ref>PMID:11344258</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Atcc 18824]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Dupin, A F]] | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: Fribourg, S]] | + | [[Category: Dupin AF]] |
| - | [[Category: 3' end mrna processing]] | + | [[Category: Fribourg S]] |
| - | [[Category: Mutant]]
| + | |
| - | [[Category: Transcription]]
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| Structural highlights
Function
CLP1_YEAST Component of the cleavage factor IA (CFIA) complex, which is involved in the endonucleolytic cleavage during polyadenylation-dependent pre-mRNA 3'-end formation and cooperates with the cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex.[1]
Publication Abstract from PubMed
Pcf11p and Clp1p form a heterodimer and are subunits of the Cleavage Factor IA (CF IA), a complex that is involved in the maturation of the 3'-end of mRNAs in Saccharomyces cerevisiae. The role of Clp1p protein in polyadenylation remains elusive, as does the need for ATP binding by Clp1p. In order to obtain structural details at atomic resolution of point mutants of Clp1p, we solved the crystal structure of Clp1-1p (G135R) point mutant complexed with Pcf11p (454-563) domain. The Clp1-1p-Pcf11p structure provides the atomic details for ATP loss while the point mutation preserves intact the Pcf11p interaction surface of Clp1p. This provides a rationale for the absence of phenotype in the yeast clp1-1 strain. Additionally, the structure allows for the description of an extended binding interface of Pcf11p with Clp1p which is likely to be S. cerevisiae specific.
Structural basis for ATP loss by Clp1p in a G135R mutant protein.,Dupin AF, Fribourg S Biochimie. 2014 Feb 5. pii: S0300-9084(14)00035-2. doi:, 10.1016/j.biochi.2014.01.017. PMID:24508575[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gross S, Moore C. Five subunits are required for reconstitution of the cleavage and polyadenylation activities of Saccharomyces cerevisiae cleavage factor I. Proc Natl Acad Sci U S A. 2001 May 22;98(11):6080-5. Epub 2001 May 8. PMID:11344258 doi:http://dx.doi.org/10.1073/pnas.101046598
- ↑ Dupin AF, Fribourg S. Structural basis for ATP loss by Clp1p in a G135R mutant protein. Biochimie. 2014 Feb 5. pii: S0300-9084(14)00035-2. doi:, 10.1016/j.biochi.2014.01.017. PMID:24508575 doi:http://dx.doi.org/10.1016/j.biochi.2014.01.017
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