4P4M

Crystal structure of Leishmania infantum polymerase beta: Ternary P/T complex

4P4M の概要

• エントリーDOI: 10.2210/pdb4p4m/pdb
• 分子名称: DNA polymerase beta, DNA (5'-D(*CP*AP*GP*TP*A)-3'), DNA (5'-D(P*AP*TP*AP*CP*TP*G)-3'), ... (7 entities in total)
• 機能のキーワード: dna polymerase, transferase-dna complex, transferase/dna
• 由来する生物種: Leishmania infantum; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 46788.22

構造登録者

Mejia, E.,Burak, M.,Alonso, A.,Larraga, V.,Kunkel, T.A.,Bebenek, K.,Garcia-Diaz, M. (登録日: 2014-03-12, 公開日: 2014-08-06, 最終更新日: 2023-09-27)

主引用文献

Mejia, E.,Burak, M.,Alonso, A.,Larraga, V.,Kunkel, T.A.,Bebenek, K.,Garcia-Diaz, M.
Structures of the Leishmania infantum polymerase beta.
DNA Repair (Amst.), 18:1-9, 2014

PubMed Abstract: Protozoans of the genus Leishmania, the pathogenic agent causing leishmaniasis, encode the family X DNA polymerase Li Pol β. Here, we report the first crystal structures of Li Pol β. Our pre- and post-catalytic structures show that the polymerase adopts the common family X DNA polymerase fold. However, in contrast to other family X DNA polymerases, the dNTP-induced conformational changes in Li Pol β are much more subtle. Moreover, pre- and post-catalytic structures reveal that Li Pol β interacts with the template strand through a nonconserved, variable region known as loop3. Li Pol β Δloop3 mutants display a higher catalytic rate, catalytic efficiency and overall error rates with respect to WT Li Pol β. These results further demonstrate the subtle structural variability that exists within this family of enzymes and provides insight into how this variability underlies the substantial functional differences among their members.

PubMed: 24666693
DOI: 10.1016/j.dnarep.2014.03.001

実験手法

X-RAY DIFFRACTION (1.9185 Å)