3c66

From Proteopedia

(Difference between revisions)

Revision as of 21:55, 25 December 2014

Yeast poly(A) polymerase in complex with Fip1 residues 80-105

Structural highlights

3c66 is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1fa0, 2o1p, 2hhp, 2q66
Gene:	PAP1, YKR002W (Saccharomyces cerevisiae)
Activity:	Polynucleotide adenylyltransferase, with EC number 2.7.7.19
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[PAP_YEAST] Polymerase 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.^[1] ^[2] [FIP1_YEAST] Polymerase-regulating 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. Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase PAP1. This inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain of PAP1. Seems to tether PAP1 to the cleavage factor I.^[3]

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

In yeast, the mRNA processing enzyme poly(A) polymerase is tethered to the much larger 3'-end processing complex via Fip1, a 36 kDa protein of unknown structure. We report the 2.6 A crystal structure of yeast poly(A) polymerase in complex with a peptide containing residues 80-105 of Fip1. The Fip1 peptide binds to the outside surface of the C-terminal domain of the polymerase. On the basis of this structure, we designed a mutant of the polymerase (V498Y, C485R) that is lethal to yeast. The mutant is unable to bind Fip1 but retains full polymerase activity. Fip1 is found in all eukaryotes and serves to connect poly(A) polymerase to pre-mRNA processing complexes in yeast, plants, and mammals. However, the Fip1 sequence is highly divergent, and residues on both Pap1 and Fip1 at the observed interaction surface are poorly conserved. Herein we demonstrate using analytical ultracentrifugation, circular dichroism, proteolytic studies, and other techniques that, in the absence of Pap1, Fip1 is largely, if not completely, unfolded. We speculate that flexibility may be important for Fip1's function as a molecular scaffold.

Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein.,Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A Biochemistry. 2008 Jul 1;47(26):6859-69. Epub 2008 Jun 7. PMID:18537269^[4]

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

References

↑ Balbo PB, Bohm A. Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis. Structure. 2007 Sep;15(9):1117-31. PMID:17850751 doi:S0969-2126(07)00283-3
↑ Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. Biochemistry. 2008 Jul 1;47(26):6859-69. Epub 2008 Jun 7. PMID:18537269 doi:10.1021/bi800204k
↑ Helmling S, Zhelkovsky A, Moore CL. Fip1 regulates the activity of Poly(A) polymerase through multiple interactions. Mol Cell Biol. 2001 Mar;21(6):2026-37. PMID:11238938 doi:http://dx.doi.org/10.1128/MCB.21.6.2026-2037.2001
↑ Meinke G, Ezeokonkwo C, Balbo P, Stafford W, Moore C, Bohm A. Structure of yeast poly(A) polymerase in complex with a peptide from Fip1, an intrinsically disordered protein. Biochemistry. 2008 Jul 1;47(26):6859-69. Epub 2008 Jun 7. PMID:18537269 doi:10.1021/bi800204k

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/3c66"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[3c66]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3C66 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3C66 FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene><br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fa0|1fa0]], [[2o1p|2o1p]], [[2hhp|2hhp]], [[2q66|2q66]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fa0|1fa0]], [[2o1p|2o1p]], [[2hhp|2hhp]], [[2q66|2q66]]</td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAP1, YKR002W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAP1, YKR002W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
-<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3c66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c66 RCSB], [http://www.ebi.ac.uk/pdbsum/3c66 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=3c66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3c66 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3c66 RCSB], [http://www.ebi.ac.uk/pdbsum/3c66 PDBsum]</span></td></tr>
-<table>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/PAP_YEAST PAP_YEAST]] Polymerase 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.<ref>PMID:17850751</ref> <ref>PMID:18537269</ref>  [[http://www.uniprot.org/uniprot/FIP1_YEAST FIP1_YEAST]] Polymerase-regulating 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. Pre-mRNA polyadenylation factor that directly interacts with poly(A) polymerase PAP1. This inhibits the extension of an oligo(A) primer by limiting access of the RNA substrate to the C-terminal RNA binding domain of PAP1. Seems to tether PAP1 to the cleavage factor I.<ref>PMID:11238938</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 38: @@
 [[Category: Polynucleotide adenylyltransferase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Bohm, A.]]
+[[Category: Bohm, A]]
-[[Category: Meinke, G.]]
+[[Category: Meinke, G]]
 [[Category: Mrna processing]]
 [[Category: Nucleus]]

3c66

From Proteopedia

Revision as of 21:55, 25 December 2014

Yeast poly(A) polymerase in complex with Fip1 residues 80-105

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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