Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic ψχ heterodimer | Zendy

Farzaneh Tondnevis | Zendy; Richard E. Gillilan | Zendy; Linda B. Bloom | Zendy; Robert McKenna | Zendy

Open Access

Solution study of the Escherichia coli DNA polymerase III clamp loader reveals the location of the dynamic ψχ heterodimer

Author(s) -

Farzaneh Tondnevis,

Richard E. Gillilan,

Linda B. Bloom,

Robert McKenna

Publication year - 2015

Publication title -

structural dynamics

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.415

H-Index - 29

ISSN - 2329-7778

DOI - 10.1063/1.4927407

Subject(s) - loader , clamp , protein subunit , dna clamp , dna , core (optical fiber) , dna polymerase , chemistry , crystallography , escherichia coli , physics , polymerase chain reaction , computer science , biochemistry , gene , reverse transcriptase , optics , clamping , computer vision , operating system

Several X-ray crystal structures of the E. coli core clamp loader containing the five core (δ′, δ, and three truncated γ) subunits have been determined, but they lack the ψ and χ subunits. We report the first solution structure of the complete seven-subunit clamp loader complex using small angle X-ray scattering. This structure not only provides information about the location of the χ and ψ subunits but also provides a model of the dynamic nature of the clamp loader complex

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