2BPF

STRUCTURES OF TERNARY COMPLEXES OF RAT DNA POLYMERASE BETA, A DNA TEMPLATE-PRIMER, AND DDCTP

2BPF の概要

• エントリーDOI: 10.2210/pdb2bpf/pdb
• 関連するPDBエントリー: 2BPG
• 分子名称: DNA (5'-D(*GP*GP*GP*CP*GP*CP*CP*G)-3'), DNA (5'-D(*CP*GP*GP*CP*GP*CP*C)-3'), PROTEIN (DNA POLYMERASE BETA (E.C.2.7.7.7)), ... (6 entities in total)
• 機能のキーワード: protein-dna complex, transferase-dna complex, transferase/dna
• 由来する生物種: Rattus norvegicus (Norway rat)
• 細胞内の位置: Nucleus: P06766
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 43456.53

構造登録者

Pelletier, H.,Sawaya, M.R.,Kumar, A.,Wilson, S.H.,Kraut, J. (登録日: 1994-05-19, 公開日: 1994-12-14, 最終更新日: 2024-02-14)

主引用文献

Pelletier, H.,Sawaya, M.R.,Kumar, A.,Wilson, S.H.,Kraut, J.
Structures of ternary complexes of rat DNA polymerase beta, a DNA template-primer, and ddCTP.
Science, 264:1891-1903, 1994

PubMed Abstract: Two ternary complexes of rat DNA polymerase beta (pol beta), a DNA template-primer, and dideoxycytidine triphosphate (ddCTP) have been determined at 2.9 A and 3.6 A resolution, respectively. ddCTP is the triphosphate of dideoxycytidine (ddC), a nucleoside analog that targets the reverse transcriptase of human immunodeficiency virus (HIV) and is at present used to treat AIDS. Although crystals of the two complexes belong to different space groups, the structures are similar, suggesting that the polymerase-DNA-ddCTP interactions are not affected by crystal packing forces. In the pol beta active site, the attacking 3'-OH of the elongating primer, the ddCTP phosphates, and two Mg2+ ions are all clustered around Asp190, Asp192, and Asp256. Two of these residues, Asp190 and Asp256, are present in the amino acid sequences of all polymerases so far studied and are also spatially similar in the four polymerases--the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, T7 RNA polymerase, and rat DNA pol beta--whose crystal structures are now known. A two-metal ion mechanism is described for the nucleotidyl transfer reaction and may apply to all polymerases. In the ternary complex structures analyzed, pol beta binds to the DNA template-primer in a different manner from that recently proposed for other polymerase-DNA models.

PubMed: 7516580

実験手法

X-RAY DIFFRACTION (2.9 Å)