Poly(A) Polymerase

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[[Image:2q66.gif|left|200px]]<br /><applet load="2q66" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2q66.gif|left|200px]]
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caption="2q66, resolution 1.800&Aring;" />
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'''Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)'''<br />
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{{Structure
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|PDB= 2q66 |SIZE=350|CAPTION= <scene name='initialview01'>2q66</scene>, resolution 1.800&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene> and <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>
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|ACTIVITY= [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]
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|GENE= PAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2Q66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=ATP:'>ATP</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Q66 OCA].
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2Q66 is a [[Single protein]] structure of 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=2Q66 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17850751 17850751]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/17850751 17850751]
[[Category: Polynucleotide adenylyltransferase]]
[[Category: Polynucleotide adenylyltransferase]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: transferase/rna complex]]
[[Category: transferase/rna complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:36:25 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:22:12 2008''

Revision as of 16:22, 20 March 2008


PDB ID 2q66

Drag the structure with the mouse to rotate
, resolution 1.800Å
Ligands: , and
Gene: PAP1 (Saccharomyces cerevisiae)
Activity: Polynucleotide adenylyltransferase, with EC number 2.7.7.19
Coordinates: save as pdb, mmCIF, xml



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


Overview

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.

About this Structure

2Q66 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

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

Page seeded by OCA on Thu Mar 20 18:22:12 2008

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