Structure of DNA polymerase I Klenow fragment bound to duplex DNA.

Science (1993), Volume 260, Page 352


Klenow fragment of Escherichia coli DNA polymerase I, which was cocrystallized with duplex DNA, positioned 11 base pairs of DNA in a groove that lies at right angles to the cleft that contains the polymerase active site and is adjacent to the 3' to 5' exonuclease domain. When the fragment bound DNA, a region previously referred to as the "disordered domain" became more ordered and moved along with two helices toward the 3' to 5' exonuclease domain to form the binding groove. A single-stranded, 3' extension of three nucleotides bound to the 3' to 5' exonuclease active site. Although this cocrystal structure appears to be an editing complex, it suggests that the primer strand approaches the catalytic site of the polymerase from the direction of the 3' to 5' exonuclease domain and that the duplex DNA product may bend to enter the cleft that contains the polymerase catalytic site.



Structure and Structure/Function

One line summary:

Cocrystal structure of KF with frayed duplex DNA having 3' end in the exo site


D355A mutant (exo-minus) PDB file 1KLN


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Polymerase Reference Property Result Context
Klenow fragment Beese LS1993 Residues Involved in Catalysis of 3-5' Exo D355, E357, D424, D501
Klenow fragment Beese LS1993 Amino Acids Contacting Template N579, S582, D827, R835
Klenow fragment Beese LS1993 Other Important Residues L361, Q419, R455, F473, Y497, H660, T609, E611, R631, K635, N675, N678

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