2bf0

From Proteopedia

(Difference between revisions)

Revision as of 11:21, 22 May 2024

crystal structure of the rpr of pcf11

Structural highlights

2bf0 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.3Å
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PCF11_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 cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.^[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

The C-terminal domain (CTD) of the large subunit of RNA polymerase II is a platform for mRNA processing factors and links gene transcription to mRNA capping, splicing and polyadenylation. Pcf11, an essential component of the mRNA cleavage factor IA, contains a CTD-interaction domain that binds in a phospho-dependent manner to the heptad repeats within the RNA polymerase II CTD. We show here that the phosphorylated CTD exists as a dynamic disordered ensemble in solution and, by induced fit, it assumes a structured conformation when bound to Pcf11. In addition, we detected cis-trans populations for the CTD prolines, and found that only the all-trans form is selected for binding. These data suggest that the recognition of the CTD is regulated by independent site-specific modifications (phosphorylation and proline cis-trans isomerization) and, probably, by the local concentration of suitable binding sites.

Key features of the interaction between Pcf11 CID and RNA polymerase II CTD.,Noble CG, Hollingworth D, Martin SR, Ennis-Adeniran V, Smerdon SJ, Kelly G, Taylor IA, Ramos A Nat Struct Mol Biol. 2005 Feb;12(2):144-51. Epub 2005 Jan 16. PMID:15665873^[3]

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
↑ Zhang Z, Fu J, Gilmour DS. CTD-dependent dismantling of the RNA polymerase II elongation complex by the pre-mRNA 3'-end processing factor, Pcf11. Genes Dev. 2005 Jul 1;19(13):1572-80. PMID:15998810 doi:http://dx.doi.org/19/13/1572
↑ Noble CG, Hollingworth D, Martin SR, Ennis-Adeniran V, Smerdon SJ, Kelly G, Taylor IA, Ramos A. Key features of the interaction between Pcf11 CID and RNA polymerase II CTD. Nat Struct Mol Biol. 2005 Feb;12(2):144-51. Epub 2005 Jan 16. PMID:15665873 doi:10.1038/nsmb887

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/2bf0"

@@ Line 3: / Line 3: @@
 <StructureSection load='2bf0' size='340' side='right'caption='[[2bf0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2bf0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2bf0]] is a 1 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=2BF0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BF0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></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]] 2.3&#8491;</td></tr>
-<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1sz9|1sz9]], [[1sza|1sza]]</div></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=2bf0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bf0 OCA], [https://pdbe.org/2bf0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bf0 RCSB], [https://www.ebi.ac.uk/pdbsum/2bf0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bf0 ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/PCF11_YEAST PCF11_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 cleavage factor NAB4/CFIB and the cleavage and polyadenylation factor (CPF) complex. Independently involved in RNA polymerase II transcript termination. Binds RNA. Seems to bridge RNA polymerase II and the native transcript and may be involved in dismantling the RNA polymerase II elongation complex.<ref>PMID:11344258</ref> <ref>PMID:15998810</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 33: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Adeniran, V E]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Hollingworth, D]]
+[[Category: Adeniran VE]]
-[[Category: Kelly, G]]
+[[Category: Hollingworth D]]
-[[Category: Martin, S R]]
+[[Category: Kelly G]]
-[[Category: Noble, C G]]
+[[Category: Martin SR]]
-[[Category: Ramos, A]]
+[[Category: Noble CG]]
-[[Category: Smerdon, S J]]
+[[Category: Ramos A]]
-[[Category: Taylor, I A]]
+[[Category: Smerdon SJ]]
-[[Category: Phosphorylation]]
+[[Category: Taylor IA]]
-[[Category: Rna]]
-[[Category: Transcription]]

2bf0

From Proteopedia

Revision as of 11:21, 22 May 2024

crystal structure of the rpr of pcf11

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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