6K9C

The apo structure of NrS-1 C terminal region (305-718)

Summary for 6K9C

• Entry DOI: 10.2210/pdb6k9c/pdb
• Descriptor: Primase, MERCURY (II) ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: primase, helicase, ssdna-binding protein, transferase
• Biological source: Nitratiruptor phage NrS-1
• Total number of polymer chains: 2
• Total formula weight: 97597.21

Authors

Chen, X.,Gan, J. (deposition date: 2019-06-14, release date: 2020-04-08, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.406 Å)