Poly(A) Polymerase: Difference between revisions
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[[Image:2q66.gif|left|200px]]<br /><applet load="2q66" size=" | [[Image:2q66.gif|left|200px]]<br /><applet load="2q66" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2q66, resolution 1.800Å" /> | caption="2q66, resolution 1.800Å" /> | ||
'''Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)'''<br /> | '''Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
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 MG, ATP and EDO 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:// | 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]. | ||
==Reference== | ==Reference== | ||
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[[Category: transferase/rna complex]] | [[Category: transferase/rna complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 12:34:17 2008'' | ||
Revision as of 13:34, 23 January 2008
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Structure of Yeast Poly(A) Polymerase with ATP and oligo(A)
OverviewOverview
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 StructureAbout this Structure
2Q66 is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Active as Polynucleotide adenylyltransferase, with EC number 2.7.7.19 Full crystallographic information is available from OCA.
ReferenceReference
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
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