5VTP

X-ray diffraction data of DNA Polymerase Eta (RAD30) of Saccharomyces cerevisiae with a single magnesium bound in absence of DNA and incoming dNTP

5VTP の概要

• エントリーDOI: 10.2210/pdb5vtp/pdb
• 分子名称: DNA polymerase eta, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: rad30, dna polymerase eta, dna transferase, catalytic domain, transferase
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 60856.35

構造登録者

Powers, K.T.,Washington, M.T. (登録日: 2017-05-17, 公開日: 2018-01-24, 最終更新日: 2023-10-04)

主引用文献

Powers, K.T.,Elcock, A.H.,Washington, M.T.
The C-terminal region of translesion synthesis DNA polymerase eta is partially unstructured and has high conformational flexibility.
Nucleic Acids Res., 46:2107-2120, 2018

PubMed Abstract: Eukaryotic DNA polymerase η catalyzes translesion synthesis of thymine dimers and 8-oxoguanines. It is comprised of a polymerase domain and a C-terminal region, both of which are required for its biological function. The C-terminal region mediates interactions with proliferating cell nuclear antigen (PCNA) and other translesion synthesis proteins such as Rev1. This region contains a ubiquitin-binding/zinc-binding (UBZ) motif and a PCNA-interacting protein (PIP) motif. Currently little structural information is available for this region of polymerase η. Using a combination of approaches-including genetic complementation assays, X-ray crystallography, Langevin dynamics simulations, and small-angle X-ray scattering-we show that the C-terminal region is partially unstructured and has high conformational flexibility. This implies that the C-terminal region acts as a flexible tether linking the polymerase domain to PCNA thereby increasing its local concentration. Such tethering would facilitate the sampling of translesion synthesis polymerases to ensure that the most appropriate one is selected to bypass the lesion.

PubMed: 29385534
DOI: 10.1093/nar/gky031

実験手法

X-RAY DIFFRACTION (2.8 Å)