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Science 16 April 1993:
Vol. 260. no. 5106, pp. 352 - 355
DOI: 10.1126/science.8469987
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Articles

Science, Vol 260, Issue 5106, 352-355
Copyright © 1993 by American Association for the Advancement of Science

articles

Structure of DNA polymerase I Klenow fragment bound to duplex DNA

LS Beese, V Derbyshire, and TA Steitz

Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.

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.


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