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- W3137931202 abstract "The E. coli γ clamp loader is a pentameric complex of δ, δ' and three γ subunits that opens and loads β-clamp proteins onto DNA in an ATP-dependent process essential for efficient DNA replication. ATP binding to the γ subunits promotes conformational changes that enable the clamp loader to bind and open the ring-shaped β-clamp homodimer. Here we report the nearly complete backbone and side-chain 1H, 13C and 15N NMR resonance assignments of the 242-residue truncated γ subunit of the clamp loader complex, which includes the N-terminal mini (domain I) and lid (domain II) domains. This construct represents the nucleotide binding module in the clamp loader complex and provides a model system for studies of conformational rearrangements of the clamp loader induced by nucleotide binding." @default.
- W3137931202 created "2021-03-29" @default.
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- W3137931202 date "2021-03-24" @default.
- W3137931202 modified "2023-10-08" @default.
- W3137931202 title "NMR resonance assignments for the nucleotide binding domains of the E. coli clamp loader complex γ subunit" @default.
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- W3137931202 doi "https://doi.org/10.1007/s12104-021-10018-7" @default.
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