title: An open and closed case for all polymerases.
abstract: The recently determined structures of HIV-1 reverse transcriptase and Taq DNA polymerase in complex with DNA primer-template and an incoming nucleotide have shown that a large conformational change configures the polymerase active site for nucleotidyl transfer. The structure of reverse transcriptase in the catalytic complex will open the path to the rational design of novel nucleoside analog inhibitors of viral replication.
authors.affiliation: Department of Microbiology and Molecular Genetics, The Markey Center for Molecular Genetics, University of Vermont, Burlington, VT 05405, USA.
authors.forename: S
authors.initials: S
authors.lastname: Doublié
authors.forename: M R
authors.initials: MR
authors.lastname: Sawaya
authors.forename: T
authors.initials: T
authors.lastname: Ellenberger
mesh_terms: D001665:Binding Sites; D017931:DNA Primers / Q000737:chemistry; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry*; D054303:HIV Reverse Transcriptase / Q000737:chemistry; D015497:HIV-1 / Q000201:enzymology*; D008958:Models, Molecular; D017433:Protein Structure, Secondary; D019914:Taq Polymerase / Q000737:chemistry
chemical_list: D017931:DNA Primers; D019914:Taq Polymerase; D054303:HIV Reverse Transcriptase; D004259:DNA-Directed DNA Polymerase