Poly(A) Polymerase
From Proteopedia
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|PDB= 2q66 |SIZE=350|CAPTION= <scene name='initialview01'>2q66</scene>, resolution 1.800Å | |PDB= 2q66 |SIZE=350|CAPTION= <scene name='initialview01'>2q66</scene>, resolution 1.800Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=A:ADENOSINE-5'-MONOPHOSPHATE'>A</scene>, <scene name='pdbligand=ATP:ADENOSINE-5'-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
| - | |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] | + | |ACTIVITY= <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> |
|GENE= PAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= PAP1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<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://www.ebi.ac.uk/pdbsum/2q66 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2q66 RCSB]</span> | ||
}} | }} | ||
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[[Category: Balbo, P.]] | [[Category: Balbo, P.]] | ||
[[Category: Bohm, A.]] | [[Category: Bohm, A.]] | ||
| - | [[Category: ATP]] | ||
| - | [[Category: EDO]] | ||
| - | [[Category: MG]] | ||
[[Category: protein rna complex atp polymerase complex]] | [[Category: protein rna complex atp polymerase complex]] | ||
[[Category: transferase/rna complex]] | [[Category: transferase/rna complex]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:45:16 2008'' |
Revision as of 01:45, 31 March 2008
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| , resolution 1.800Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Gene: | PAP1 (Saccharomyces cerevisiae) | ||||||
| Activity: | Polynucleotide adenylyltransferase, with EC number 2.7.7.19 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Mon Mar 31 04:45:16 2008
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Eran Hodis, David Canner, Joel L. Sussman, OCA, Alexander Berchansky, Jaime Prilusky, David S. Goodsell, Eric Martz
