6M40

Crystal structure of the NS3-like helicase from Alongshan virus

Summary for 6M40

• Entry DOI: 10.2210/pdb6m40/pdb
• Related: 5JMT
• Descriptor: NS3-like protein (1 entity in total)
• Functional Keywords: ms3, helicase, alsv, flavivirus, viral protein
• Biological source: Alongshan virus
• Total number of polymer chains: 1
• Total formula weight: 55212.88

Authors

Gao, X.P.,Zhu, K.X.,Chen, P.,Wojdyla, J.A.,Wang, M.,Cui, S. (deposition date: 2020-03-05, release date: 2020-04-08, Last modification date: 2024-11-13)

Primary citation

Gao, X.,Zhu, K.,Wojdyla, J.A.,Chen, P.,Qin, B.,Li, Z.,Wang, M.,Cui, S.
Crystal structure of the NS3-like helicase from Alongshan virus.
Iucrj, 7:375-382, 2020

PubMed Abstract: Alongshan virus (ALSV) is an emerging human pathogen that was identified in China and rapidly spread to the European continent in 2019, raising concerns about public health. ALSV belongs to the distinct group within the family with segmented RNA genomes. While segments 2 and 4 of the ALSV genome encode the VP1-VP3 proteins of unknown origin, segments 1 and 3 encode the NS2b-NS3 and NS5 proteins, which are related to nonstructural proteins, suggesting an evolutionary link between segmented and unsegmented viruses within the family. Here, the enzymatic activity of the ALSV NS3-like helicase (NS3-Hel) was characterized and its crystal structure was determined to 2.9 Å resolution. ALSV NS3-Hel exhibits an ATPase activity that is comparable to those measured for NS3 helicases. The structure of ALSV NS3-Hel exhibits an overall fold similar to those of NS3 helicases. Despite the limited amino-acid sequence identity between ALSV NS3-Hel and NS3 helicases, structural features at the ATPase active site and the RNA-binding groove remain conserved in ALSV NS3-Hel. These findings provide a structural framework for drug design and suggest the possibility of developing a broad-spectrum antiviral drug against both and .

PubMed: 32431821
DOI: 10.1107/S2052252520003632

Experimental method

X-RAY DIFFRACTION (2.89 Å)