Crystal structure of the catalytic [alpha] subunit of E. coli replicative DNA Polymerase lll

Article Abstract:

The independent growth of the DNA replication machinery in bacteria is suggested by the significant difference in structure between Polymerase lll (Pol III) and the members of the canonical DNA polymerase families that include eukaroyotic replicative polymerase. The likelihood that all DNA polymerases share a common ancestor is suggested by a structural element near the active site in Pol lll, also highlighting a model for interaction of Pol lll with the sliding clamp and DNA.ddna replicatiopn

Science & research, Research, Genetic aspects, Escherichia coli, DNA replication

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Structure of the C-terminal region of p21WAF1/CIP1 complexed with human PCNA

Article Abstract:

The binding functionality of the human proliferating cell nuclear antigen (PCNA) with p21WAF1/CIP1 complex is located on the C-terminal 22 residue which blocks PCNA-mediated gene replication. The PCNA-p21 complex exhibits a trigonal crystal structure in which one 22 residue peptide is bonded with three PCNA subunits. The complex is composed of 57% peptide and 43% PCNA that form a ring with an uncovered hole in its center.

Analysis, Proteins, Chromosome replication, Protein structure, Recombinant proteins

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Similar abstracts:

• Abstracts: Crystal structure of the delta subunit of the clamp-loader complex of E. colin DNA polymerase III. Mechanism of processivity clamp opening by the delta subunit wrench of the clamp loader complex of E. coli DNA polymerase III

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