1IM4

Crystal Structure of a DinB Homolog (DBH) Lesion Bypass DNA Polymerase Catalytic Fragment from Sulfolobus solfataricus

1IM4 の概要

• エントリーDOI: 10.2210/pdb1im4/pdb
• 分子名称: DBH, SULFATE ION (3 entities in total)
• 機能のキーワード: dna polymerase palm, thumb, fingers, helix-hairpin-helix, fidelity, processivity, transferase
• 由来する生物種: Sulfolobus solfataricus
• 細胞内の位置: Cytoplasm (Probable): P96022
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 25124.98

構造登録者

Pata, J.D.,Zhou, B.L.,Steitz, T.A. (登録日: 2001-05-09, 公開日: 2001-09-12, 最終更新日: 2024-02-07)

主引用文献

Zhou, B.L.,Pata, J.D.,Steitz, T.A.
Crystal structure of a DinB lesion bypass DNA polymerase catalytic fragment reveals a classic polymerase catalytic domain.
Mol.Cell, 8:427-437, 2001

PubMed Abstract: The UmuC/DinB family of bypass polymerases is responsible for translesion DNA synthesis and includes the human polymerases eta, iota, and kappa. We determined the 2.3 A resolution crystal structure of a catalytic fragment of the DinB homolog (Dbh) polymerase from Sulfolobus solfataricus and show that it is nonprocessive and can bypass an abasic site. The structure of the catalytic domain is nearly identical to those of most other polymerase families. Homology modeling suggests that there is minimal contact between protein and DNA, that the nascent base pair binding pocket is quite accessible, and that the enzyme is already in a closed conformation characteristic of ternary polymerase complexes. These observations afford insights into the sources of low fidelity and low processivity of the UmuC/DinB polymerases.

PubMed: 11545744
DOI: 10.1016/S1097-2765(01)00310-0

実験手法

X-RAY DIFFRACTION (2.3 Å)