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| | <StructureSection load='1fa0' size='340' side='right'caption='[[1fa0]], [[Resolution|resolution]] 2.60Å' scene=''> | | <StructureSection load='1fa0' size='340' side='right'caption='[[1fa0]], [[Resolution|resolution]] 2.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1fa0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. The October 2008 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Poly(A) Polymerase'' by David Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2008_10 10.2210/rcsb_pdb/mom_2008_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FA0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1fa0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. The October 2008 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Poly(A) Polymerase'' by David Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2008_10 10.2210/rcsb_pdb/mom_2008_10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FA0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FA0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=3AD:3-DEOXYADENOSINE'>3AD</scene>, <scene name='pdbligand=3AT:3-DEOXYADENOSINE-5-TRIPHOSPHATE'>3AT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3AD:3-DEOXYADENOSINE'>3AD</scene>, <scene name='pdbligand=3AT:3-DEOXYADENOSINE-5-TRIPHOSPHATE'>3AT</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=POP:PYROPHOSPHATE+2-'>POP</scene></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 id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Polynucleotide_adenylyltransferase Polynucleotide adenylyltransferase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.7.19 2.7.7.19] </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=1fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa0 OCA], [http://pdbe.org/1fa0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fa0 RCSB], [http://www.ebi.ac.uk/pdbsum/1fa0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa0 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=1fa0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fa0 OCA], [https://pdbe.org/1fa0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fa0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fa0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fa0 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == 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> | + | [[https://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> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Structural highlights
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]
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
Polyadenylate [poly(A)] polymerase (PAP) catalyzes the addition of a polyadenosine tail to almost all eukaryotic messenger RNAs (mRNAs). The crystal structure of the PAP from Saccharomyces cerevisiae (Pap1) has been solved to 2.6 angstroms, both alone and in complex with 3'-deoxyadenosine triphosphate (3'-dATP). Like other nucleic acid polymerases, Pap1 is composed of three domains that encircle the active site. The arrangement of these domains, however, is quite different from that seen in polymerases that use a template to select and position their incoming nucleotides. The first two domains are functionally analogous to polymerase palm and fingers domains. The third domain is attached to the fingers domain and is known to interact with the single-stranded RNA primer. In the nucleotide complex, two molecules of 3'-dATP are bound to Pap1. One occupies the position of the incoming base, prior to its addition to the mRNA chain. The other is believed to occupy the position of the 3' end of the mRNA primer.
Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP.,Bard J, Zhelkovsky AM, Helmling S, Earnest TN, Moore CL, Bohm A Science. 2000 Aug 25;289(5483):1346-9. PMID:10958780[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
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
- ↑ Bard J, Zhelkovsky AM, Helmling S, Earnest TN, Moore CL, Bohm A. Structure of yeast poly(A) polymerase alone and in complex with 3'-dATP. Science. 2000 Aug 25;289(5483):1346-9. PMID:10958780
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