1BPB

CRYSTAL STRUCTURE OF RAT DNA POLYMERASE BETA: EVIDENCE FOR A COMMON POLYMERASE MECHANISM

1BPB の概要

• エントリーDOI: 10.2210/pdb1bpb/pdb
• 分子名称: DNA POLYMERASE BETA (2 entities in total)
• 機能のキーワード: nucleotidyltransferase
• 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: 1
• 化学式量合計: 28774.53

構造登録者

Sawaya, M.R.,Pelletier, H.,Kumar, A.,Wilson, S.H.,Kraut, J. (登録日: 1994-04-12, 公開日: 1994-06-22, 最終更新日: 2024-02-07)

主引用文献

Sawaya, M.R.,Pelletier, H.,Kumar, A.,Wilson, S.H.,Kraut, J.
Crystal structure of rat DNA polymerase beta: evidence for a common polymerase mechanism.
Science, 264:1930-1935, 1994

PubMed Abstract: Structures of the 31-kilodalton catalytic domain of rat DNA polymerase beta (pol beta) and the whole 39-kilodalton enzyme were determined at 2.3 and 3.6 angstrom resolution, respectively. The 31-kilodalton domain is composed of fingers, palm, and thumb subdomains arranged to form a DNA binding channel reminiscent of the polymerase domains of the Klenow fragment of Escherichia coli DNA polymerase I, HIV-1 reverse transcriptase, and bacteriophage T7 RNA polymerase. The amino-terminal 8-kilodalton domain is attached to the fingers subdomain by a flexible hinge. The two invariant aspartates found in all polymerase sequences and implicated in catalytic activity have the same geometric arrangement within structurally similar but topologically distinct palms, indicating that the polymerases have maintained, or possibly re-evolved, a common nucleotidyl transfer mechanism. The location of Mn2+ and deoxyadenosine triphosphate in pol beta confirms the role of the invariant aspartates in metal ion and deoxynucleoside triphosphate binding.

PubMed: 7516581

実験手法

X-RAY DIFFRACTION (2.3 Å)