5D46

Structural Basis for a New Templated Activity by Terminal Deoxynucleotidyl Transferase: Implications for V(D)J Recombination

5D46 の概要

• エントリーDOI: 10.2210/pdb5d46/pdb
• 分子名称: Terminal deoxynucleotidyltransferase, DNA (5'-D(*AP*AP*AP*AP*AP*A)-3'), DNA (5'-D(*TP*TP*TP*TP*TP*GP*C)-3'), ... (9 entities in total)
• 機能のキーワード: tdt, synapsis, double strand breaks, transferase
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 54105.82

構造登録者

Loc'h, J.,Rosario, S.,Delarue, M. (登録日: 2015-08-07, 公開日: 2016-07-27, 最終更新日: 2024-01-10)

主引用文献

Loc'h, J.,Rosario, S.,Delarue, M.
Structural Basis for a New Templated Activity by Terminal Deoxynucleotidyl Transferase: Implications for V(D)J Recombination.
Structure, 24:1452-1463, 2016

PubMed Abstract: Eukaryotic DNA polymerase of the polX family, such as pol μ and terminal deoxynucleotidyl transferase (TdT), are key components of the non-homologous end-joining or V(D)J recombination machinery, respectively. The established role of TdT is to add random nucleotides during V(D)J recombination. Here we show that TdT also has a templated-polymerase activity, similar to pol μ, in the presence of higher concentrations of a downstream DNA duplex, and performs a micro-homology single base-pair search to align the DNA synapsis. To understand the molecular basis of this alignment, we solve crystal structures of TdT with four DNA strands and study the influence of the 3' protruding end. Two mutations in TdT inspired by sequence alignments with pol μ further improve the templated activity. We propose that both templated and untemplated activities of TdT are needed to explain the distributions of lengths of N regions observed experimentally in T cell receptors and antibodies.

PubMed: 27499438
DOI: 10.1016/j.str.2016.06.014

実験手法

X-RAY DIFFRACTION (2.8 Å)