6LRB

The A form apo structure of NrS-1 C terminal region-CTR

6LRB の概要

• エントリーDOI: 10.2210/pdb6lrb/pdb
• 分子名称: Primase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: primase, helicase, ssdna-binding prorein, hydrolase
• 由来する生物種: Nitratiruptor phage NrS-1
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 290195.74

構造登録者

Chen, X.,Gan, J. (登録日: 2020-01-15, 公開日: 2020-04-08, 最終更新日: 2023-11-29)

主引用文献

Chen, X.,Su, S.,Chen, Y.,Gao, Y.,Li, Y.,Shao, Z.,Zhang, Y.,Shao, Q.,Liu, H.,Li, J.,Ma, J.,Gan, J.
Structural studies reveal a ring-shaped architecture of deep-sea vent phage NrS-1 polymerase.
Nucleic Acids Res., 48:3343-3355, 2020

PubMed Abstract: NrS-1 is the first known phage that can infect Epsilonproteobacteria, one of the predominant primary producers in the deep-sea hydrothermal vent ecosystems. NrS-1 polymerase is a multidomain enzyme and is one key component of the phage replisome. The N-terminal Prim/Pol and HBD domains are responsible for DNA polymerization and de novo primer synthesis activities of NrS-1 polymerase. However, the structure and function of the C-terminus (CTR) of NrS-1 polymerase are poorly understood. Here, we report two crystal structures, showing that NrS-1 CTR adopts one unique hexameric ring-shaped conformation. Although the central helicase domain of NrS-1 CTR shares structural similarity with the superfamily III helicases, the folds of the Head and Tail domains are completely novel. Via mutagenesis and in vitro biochemical analysis, we identified many residues important for the helicase and polymerization activities of NrS-1 polymerase. In addition to NrS-1 polymerase, our study may also help us identify and understand the functions of multidomain polymerases expressed by many NrS-1 related phages.

PubMed: 32016421
DOI: 10.1093/nar/gkaa071

実験手法

X-RAY DIFFRACTION (2.65 Å)