1KFD

CRYSTAL STRUCTURES OF THE KLENOW FRAGMENT OF DNA POLYMERASE I COMPLEXED WITH DEOXYNUCLEOSIDE TRIPHOSPHATE AND PYROPHOSPHATE

1KFD の概要

• エントリーDOI: 10.2210/pdb1kfd/pdb
• 分子名称: DNA POLYMERASE I KLENOW FRAGMENT, CYTIDINE-5'-TRIPHOSPHATE (2 entities in total)
• 機能のキーワード: nucleotidyltransferase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 68644.84

構造登録者

Beese, L.S.,Friedman, J.M.,Steitz, T.A. (登録日: 1993-09-23, 公開日: 1994-06-22, 最終更新日: 2024-02-07)

主引用文献

Beese, L.S.,Friedman, J.M.,Steitz, T.A.
Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate.
Biochemistry, 32:14095-14101, 1993

PubMed Abstract: Crystal 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. The dNTP binds adjacent to the O-helix [Ollis, D. L., Brick, P., Hamlin, R., Xuong, N. G., & Steitz, T. A. (1985a) Nature 313, 762-766] with its triphosphate moiety anchored by three positively charged residues, Arg 754, Arg 682, and Lys 758, plus His 734 and Gln 708. 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 [Polesky, A. H., Steitz, T. A., Grindley, N. D. F., & Joyce, C. M. (1990) J. Biol. Chem. 265, 14579-14591; Polesky, A. H., Dahlberg, M. E., Benkovic, S. J., Grindley, N. D. F., & Joyce, C. M. (1992) J. Biol. Chem. 267, 8417-8428]. 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.

PubMed: 8260491
DOI: 10.1021/bi00214a004

実験手法

X-RAY DIFFRACTION (3.9 Å)