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- W2093072087 abstract "The γ complex, an AAA+ ATPase, is the bacterial homolog of eukaryotic replication factor C (RFC) that loads the sliding clamp (β, homologous to PCNA) onto DNA. The 2.7/3.0 Å crystal structure of γ complex reveals a pentameric arrangement of subunits, with stoichiometry δ′:γ3:δ. The C-terminal domains of the subunits form a circular collar that supports an asymmetric arrangement of the N-terminal ATP binding domains of the γ motor and the structurally related domains of the δ′ stator and the δ wrench. The structure suggests a mechanism by which the γ complex switches between a closed state, in which the β-interacting element of δ is hidden by δ′, and an open form similar to the crystal structure, in which δ is free to bind to β." @default.
- W2093072087 created "2016-06-24" @default.
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- W2093072087 date "2001-08-01" @default.
- W2093072087 modified "2023-10-02" @default.
- W2093072087 title "Crystal Structure of the Processivity Clamp Loader Gamma (γ) Complex of E. coli DNA Polymerase III" @default.
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- W2093072087 doi "https://doi.org/10.1016/s0092-8674(01)00463-9" @default.
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