Crystal structure of the delta subunit of the clamp-loader complex of E. colin DNA polymerase III

Article Abstract:

The three domains in the crystal structure of the delta' subunit of the clamp-loader complex of E. coli DNA polymerase III, are arranged in a C-shape. A nonfunctional nucleotide binding site is contained in the N-terminal domain. It is indicated that nucleotides bind to the gamma subunit, which is the catalytic part of the clamp-load complex, at an interdomain interface within the C.

Observations

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Crystal structure of the processivity clamp loader gamma complex of E. coli DNA polymerase III

Article Abstract:

Crystallographic analysis of the clamp loader gamma complex of Escherichia coli DNA polymerase III shows a pentameric arrangement of subunits with their C-terminal domains forming a circular collar and the N-terminal domains binding ATP. The structure indicates that the gamma complex switches between a closed state and an open form.

Proteins, Structure-activity relationships (Biochemistry), Protein structure

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Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III

Article Abstract:

The structure of the beta:delta complex of the clamp loader complex of Escherichia coli DNA polymerase complex III reveals that the clamp loader opens by the interaction between the beta dimer and the delta wrench, which opens the beta ring.

DNA, Conformational analysis, DNA-ligand interactions, DNA binding

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