7T1B

Rev1 Ternary Complex with rCTP and Ca2+

7T1B の概要

• エントリーDOI: 10.2210/pdb7t1b/pdb
• 分子名称: DNA (5'-D(P*GP*GP*GP*GP*TP*GP*TP*GP*GP*TP*AP*G)-3'), DNA (5'-D(*AP*TP*CP*GP*CP*TP*AP*CP*CP*AP*CP*AP*CP*CP*CP*C)-3'), DNA repair protein REV1, ... (7 entities in total)
• 機能のキーワード: dna polymerase, replication, transferase-dna complex, transferase/dna
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 60808.11

構造登録者

Freudenthal, B.D.,Weaver, T.M. (登録日: 2021-12-01, 公開日: 2022-05-25, 最終更新日: 2023-10-18)

主引用文献

Weaver, T.M.,Click, T.H.,Khoang, T.H.,Todd Washington, M.,Agarwal, P.K.,Freudenthal, B.D.
Mechanism of nucleotide discrimination by the translesion synthesis polymerase Rev1.
Nat Commun, 13:2876-2876, 2022

PubMed Abstract: Rev1 is a translesion DNA synthesis (TLS) polymerase involved in the bypass of adducted-guanine bases and abasic sites during DNA replication. During damage bypass, Rev1 utilizes a protein-template mechanism of DNA synthesis, where the templating DNA base is evicted from the Rev1 active site and replaced by an arginine side chain that preferentially binds incoming dCTP. Here, we utilize X-ray crystallography and molecular dynamics simulations to obtain structural insight into the dCTP specificity of Rev1. We show the Rev1 R324 protein-template forms sub-optimal hydrogen bonds with incoming dTTP, dGTP, and dATP that prevents Rev1 from adopting a catalytically competent conformation. Additionally, we show the Rev1 R324 protein-template forms optimal hydrogen bonds with incoming rCTP. However, the incoming rCTP adopts an altered sugar pucker, which prevents the formation of a catalytically competent Rev1 active site. This work provides novel insight into the mechanisms for nucleotide discrimination by the TLS polymerase Rev1.

PubMed: 35610266
DOI: 10.1038/s41467-022-30577-0

実験手法

X-RAY DIFFRACTION (1.75 Å)