Ontology highlight
ABSTRACT:
SUBMITTER: Balbo PB
PROVIDER: S-EPMC2032019 | biostudies-literature | 2007 Sep
REPOSITORIES: biostudies-literature
Structure (London, England : 1993) 20070901 9
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 subje ...[more]