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3AJF

Structural insigths into dsRNA binding and RNA silencing suppression by NS3 protein of rice hoja blanca tenuivirus

Summary for 3AJF
Entry DOI10.2210/pdb3ajf/pdb
DescriptorNon-structural protein 3, SULFATE ION (3 entities in total)
Functional Keywordsrna silencing suppression, negative strand rna virus, viral protein
Biological sourceRice hoja blanca virus
Cellular locationHost cytoplasm (By similarity): Q67897
Total number of polymer chains4
Total formula weight45510.72
Authors
Yuan, Y.A. (deposition date: 2010-06-05, release date: 2011-04-20, Last modification date: 2024-10-16)
Primary citationYang, X.,Tan, S.H.,Teh, Y.J.,Yuan, Y.A.
Structural implications into dsRNA binding and RNA silencing suppression by NS3 protein of Rice Hoja Blanca Tenuivirus
Rna, 17:903-911, 2011
Cited by
PubMed Abstract: Rice Hoja Blanca Tenuivirus (RHBV), a negative strand RNA virus, has been identified to infect rice and is widely transmitted by the insect vector. NS3 protein encoded by RHBV RNA3 was reported to be a potent RNAi suppressor to counterdefense RNA silencing in plants, insect cells, and mammalian cells. Here, we report the crystal structure of the N-terminal domain of RHBV NS3 (residues 21-114) at 2.0 Å. RHBV NS3 N-terminal domain forms a dimer by two pairs of α-helices in an anti-parallel mode, with one surface harboring a shallow groove at the dimension of 20 Å × 30 Å for putative dsRNA binding. In vitro RNA binding assay and RNA silencing suppression assay have demonstrated that the structural conserved residues located along this shallow groove, such as Arg50, His51, Lys77, and His85, participate in dsRNA binding and RNA silencing suppression. Our results provide the initial structural implications in understanding the RNAi suppression mechanism by RHBV NS3.
PubMed: 21460234
DOI: 10.1261/rna.2552811
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2 Å)
Structure validation

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