2AQ4

Ternary complex of the catalytic core of REV1 with DNA and dCTP.

2AQ4 の概要

• エントリーDOI: 10.2210/pdb2aq4/pdb
• 分子名称: 5'-D(*AP*TP*CP*CP*TP*CP*CP*CP*CP*TP*AP*C)-3', 5'-D(*TP*AP*AP*GP*GP*TP*AP*GP*GP*GP*GP*AP*GP*GP*AP*T)-3', DNA repair protein REV1, ... (6 entities in total)
• 機能のキーワード: rev1, polymerase, pad, n-digit, g-loop, transferase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• 細胞内の位置: Nucleus: P12689
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 58538.34

構造登録者

Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K. (登録日: 2005-08-17, 公開日: 2005-10-04, 最終更新日: 2024-02-14)

主引用文献

Nair, D.T.,Johnson, R.E.,Prakash, L.,Prakash, S.,Aggarwal, A.K.
Rev1 employs a novel mechanism of DNA synthesis using a protein template.
Science, 309:2219-2222, 2005

PubMed Abstract: The Rev1 DNA polymerase is highly specialized for the incorporation of C opposite template G. We present here the crystal structure of yeast Rev1 bound to template G and incoming 2'-deoxycytidine 5'-triphosphate (dCTP), which reveals that the polymerase itself dictates the identity of the incoming nucleotide, as well as the identity of the templating base. Template G and incoming dCTP do not pair with each other. Instead, the template G is evicted from the DNA helix, and it makes optimal hydrogen bonds with a segment of Rev1. Also, unlike other DNA polymerases, incoming dCTP pairs with an arginine rather than the templating base, which ensures the incorporation of dCTP over other incoming nucleotides. This mechanism provides an elegant means for promoting proficient and error-free synthesis through N2-adducted guanines that obstruct replication.

PubMed: 16195463
DOI: 10.1126/science.1116336

実験手法

X-RAY DIFFRACTION (2.32 Å)