publication . Article . Other literature type . 2007

Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis.

Paul B. Balbo; Andrew Bohm;
  • Published: 01 Sep 2007
  • Publisher: Elsevier BV
Abstract
SummaryWe report the 1.8 Å 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 ...
Subjects
free text keywords: RNA, Molecular Biology, Structural Biology, Article, Alanine, Nucleotide, chemistry.chemical_classification, chemistry, Stereochemistry, Conformational change, Polymerase, biology.protein, biology, Biochemistry, Polynucleotide adenylyltransferase, Protein structure, Ternary complex, Enzyme
Related Organizations
Abstract
SummaryWe report the 1.8 Å 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 ...
Subjects
free text keywords: RNA, Molecular Biology, Structural Biology, Article, Alanine, Nucleotide, chemistry.chemical_classification, chemistry, Stereochemistry, Conformational change, Polymerase, biology.protein, biology, Biochemistry, Polynucleotide adenylyltransferase, Protein structure, Ternary complex, Enzyme
Related Organizations
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publication . Article . Other literature type . 2007

Mechanism of poly(A) polymerase: structure of the enzyme-MgATP-RNA ternary complex and kinetic analysis.

Paul B. Balbo; Andrew Bohm;