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2q66

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Revision as of 09:39, 18 October 2017

Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)

Structural highlights

2q66 is a 2 chain structure with sequence from Atcc 18824. The October 2008 RCSB PDB Molecule of the Month feature on Poly(A) Polymerase by David Goodsell is 10.2210/rcsb_pdb/mom_2008_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Gene:	PAP1 (ATCC 18824)
Activity:	Polynucleotide adenylyltransferase, with EC number 2.7.7.19
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

We report the 1.8 A structure of yeast poly(A) polymerase (PAP) trapped in complex with ATP and a five residue poly(A) by mutation of the catalytically required aspartic acid 154 to alanine. The enzyme has undergone significant domain movement and reveals a closed conformation with extensive interactions between the substrates and all three polymerase domains. Both substrates and 31 buried water molecules are enclosed within a central cavity that is open at both ends. Four PAP mutants were subjected to detailed kinetic analysis, and studies of the adenylyltransfer (forward), pyrophosphorolysis (reverse), and nucleotidyltransfer reaction utilizing CTP for the mutants are presented. The results support a model in which binding of both poly(A) and the correct nucleotide, MgATP, induces a conformational change, resulting in formation of a stable, closed enzyme state. Thermodynamic considerations of the data are discussed as they pertain to domain closure, substrate specificity, and catalytic strategies utilized by PAP.

Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis.,Balbo PB, Bohm A Structure. 2007 Sep;15(9):1117-31. PMID:17850751^[3]

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
↑ 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

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/2q66"

@@ Line 1: / Line 1: @@
 ==Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)==
 <StructureSection load='2q66' size='340' side='right' caption='[[2q66]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</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='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=2q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q66 OCA], [http://pdbe.org/2q66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q66 RCSB], [http://www.ebi.ac.uk/pdbsum/2q66 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=2q66 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2q66 OCA], [http://pdbe.org/2q66 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2q66 RCSB], [http://www.ebi.ac.uk/pdbsum/2q66 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2q66 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 31: / Line 32: @@
 ==See Also==
-*[[Poly(A) Polymerase|Poly(A) Polymerase]]
 *[[Teaching Scenes%2C Tutorials%2C and Educators' Pages|Teaching Scenes%2C Tutorials%2C and Educators' Pages]]
 == References ==

2q66

From Proteopedia

Revision as of 09:39, 18 October 2017

Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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