Ollis, D.L., Brick, P., Hamlin, R., Xuong, N.G., Steitz, T.A.ĭepartment of Molecular Biophysics, Yale University, New Haven, Connecticut 06511. Structure of Large Fragment of Escherichia Coli DNA Polymerase I Complexed with dTMP.Synthesis of probes by random primers labeling method (2). Applications: Fill-in of 5 overhangs (1). Co-Crystal Structure of an Editing Complex of Klenow Fragment with DNAįreemont, P.S., Friedman, J.M., Beese, L.S., Steitz, T.A. DNA Polymerase I, Large (Klenow) Fragment is a DNA polymerase enzyme that lacks the 5' to 3' exonuclease activity of intact DNA Polymerase I, but does exhibit the 5' to 3' DNA polymerase and 3' to 5' exonuclease activities.Coli DNA Polymerase F: A Two Metal Ion Mechanism Structural Basis for the 3'-5' Exonuclease Activity of E.Structure of DNA Polymerase I Klenow Fragment Bound to Duplex DNAīeese, L.S., Derbyshire, V., Steitz, T.A.However, we conclude that the position of at least the dNMP moiety of dNTP in the binary complex is not likely to be the same as in its catalytically relevant complex with primer-template DNA. The dNTP binding site observed in the crystal is consistent with the results of chemical modification including cross-linking and is also near many of the amino acid residues whose mutation affects catalysis.
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The dNTP binds adjacent to the O-helix with its triphosphate moiety anchored by three positively charged residues, Arg 754, Arg 682, and Lys 758, plus His 734 and Gln 708.
Diversity, Equity, Inclusion, and AccessĬrystal structures of the Klenow fragment (KF) of DNA polymerase I from Escherichia coli complexed with deoxynucleoside triphosphate (dNTP) or with pyrophosphate (PPi) determined to 3.9-A resolution by X-ray crystallography show these molecules binding within the cleft of the polymerase domain and surrounded by residues previously implicated in dNTP binding.Citation, Usage, Privacy Policies, Logo.Biologically Interesting Molecule Reference Dictionary (BIRD).
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