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5Y3D

Structural insight into the interaction between RNA polymerase and VPg for norovirus replication

Summary for 5Y3D
Entry DOI10.2210/pdb5y3d/pdb
Related2M4G 3QID
DescriptorRNA-dependent RNA polymerase, viral protein genome-linked (VPg) (3 entities in total)
Functional Keywordsnorovirus, rna-dependent rna polymerase, vpg, interaction, viral replication, viral protein
Biological sourceMurine norovirus 1
More
Total number of polymer chains8
Total formula weight357110.60
Authors
Kim, K.H.,Lee, J.-H.,Seok, J.H. (deposition date: 2017-07-28, release date: 2018-07-18, Last modification date: 2023-11-22)
Primary citationLee, J.H.,Park, B.S.,Han, K.R.,Biering, S.B.,Kim, S.J.,Choi, J.,Seok, J.H.,Alam, I.,Chung, M.S.,Kim, H.M.,Hwang, S.,Kim, K.H.
Insight Into the Interaction Between RNA Polymerase and VPg for Murine Norovirus Replication.
Front Microbiol, 9:1466-1466, 2018
Cited by
PubMed Abstract: Norovirus (NoV) is a leading cause of epidemic acute non-bacterial gastroenteritis, and replicates through virion protein genome-linked (VPg)-primed or RNA synthesis by RNA-dependent RNA polymerase (RdRp). VPg is a multifunctional protein that plays crucial roles in viral protein translation and genome replication. However, the interaction between the RdRp and this multifunctional VPg in NoV replication has been unknown. In this study, VPg derived from murine NoV (MNV) was found to mediate the formation of higher-order multimers or tubular fibrils of MNV RdRp, which led to significantly enhanced polymerase activity . The replication of MNV mutants containing a VPg-binding defective RdRp, based on the crystal structure of an RdRp-VPg(1-73) complex, was completely blocked in a cell culture system. Our data suggest that the interaction between RdRp and VPg plays a crucial role in the multimerization-mediated RdRp activity and consequently in MNV replication, which can provide a new target of therapeutic intervention for NoV outbreaks.
PubMed: 30038601
DOI: 10.3389/fmicb.2018.01466
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.14 Å)
Structure validation

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