3UXN

Crystal Structure of Rat DNA Polymerase Beta, Wild Type Apoenzyme

3UXN の概要

• エントリーDOI: 10.2210/pdb3uxn/pdb
• 関連するPDBエントリー: 1BPB 1RPL 2BPC 3UXO 3UXP
• 分子名称: DNA polymerase beta (2 entities in total)
• 機能のキーワード: dna polymerase, base excision repair, transferase
• 由来する生物種: Rattus norvegicus (rat)
• 細胞内の位置: Nucleus: P06766
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 76777.52

構造登録者

Gridley, C.L.,Firbank, S.,Jaeger, J. (登録日: 2011-12-05, 公開日: 2012-12-05, 最終更新日: 2024-02-28)

主引用文献

Gridley, C.L.,Rangarajan, S.,Firbank, S.,Dalal, S.,Sweasy, J.B.,Jaeger, J.
Structural Changes in the Hydrophobic Hinge Region Adversely Affect the Activity and Fidelity of the I260Q Mutator DNA Polymerase beta.
Biochemistry, 52:4422-4432, 2013

PubMed Abstract: The I260Q variant of DNA polymerase β is an efficient mutator polymerase with fairly indiscriminate misincorporation activities opposite all template bases. Previous modeling studies have suggested that I260Q harbors structural variations in its hinge region. Here, we present the crystal structures of wild type and I260Q rat polymerase β in the presence and absence of substrates. Both the I260Q apoenzyme structure and the closed ternary complex with double-stranded DNA and ddTTP show ordered water molecules in the hydrophobic hinge near Gln260, whereas this is not the case in the wild type polymerase. Compared to wild type polymerase β ternary complexes, there are subtle movements around residues 260, 272, 295, and 296 in the mutant. The rearrangements in this region, coupled with side chain movements in the immediate neighborhood of the dNTP-binding pocket, namely, residues 258 and 272, provide an explanation for the altered activity and fidelity profiles observed in the I260Q mutator polymerase.

PubMed: 23651085
DOI: 10.1021/bi301368f

実験手法

X-RAY DIFFRACTION (2.5 Å)