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Báo cáo khóa học: Crystal structure of the chi:psi subassembly of the Escherichia coli DNA polymerase clamp-loader complex

Chia sẻ: Nguyen Thang | Ngày: | Loại File: PDF | Số trang:11

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The chi (v)and psi(w) subunits of Escherichia coliDNA polymerase III formaheterodimer that is associatedwith the ATP-dependent clamp-loadermachinery. InE. coli,thev:w heterodimer serves as a bridge between the clamp-loader complex and the single-strandedDNA-binding protein. We determined the crystal structure of thev:wheterodimer at 2.1 A ˚ resolution. Although neitherv(147 residues) nor w (137 residues) bind to nucleotides, the fold of each protein is similar to the folds of mononucleotide-(v) or dinucleotide-(w) binding proteins, without marked similarity to the structures of the clamp-loader subunits....

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Nội dung Text: Báo cáo khóa học: Crystal structure of the chi:psi subassembly of the Escherichia coli DNA polymerase clamp-loader complex

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