1uf2

The Atomic Structure of Rice dwarf Virus (RDV)

spinqualitylabelsall models 1uf2, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1uf2 is a 16 chain structure with sequence from Rice dwarf virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [P3_RDVA] Capsid protein which self-assembles to form the inner icosahedral capsid with a T=2 symmetry, and consisting of 60 P3 dimers. [P7_RDVO] Probable component of the transcriptional machinery present in the inner capsid. Displays dsRNA binding activity and may play an important role in the sorting of viral RNA and virion assembly. Together with the RNA-directed RNA polymerase P1 and capping enzyme P5, forms an transcriptional complex positioned near the channels situated at each of the five-fold vertices of the core. [P8_RDVO] Capsid protein which self-assembles to form the outer icosahedral capsid with a T=13 symmetry, about 70 nm in diameter and consisting of 780 molecules capsid proteins. Publication Abstract from PubMed Rice dwarf virus (RDV), the causal agent of rice dwarf disease, is a member of the genus Phytoreovirus in the family Reoviridae. RDV is a double-shelled virus with a molecular mass of approximately 70 million Dalton. This virus is widely prevalent and is one of the viruses that cause the most economic damage in many Asian countries. The atomic structure of RDV was determined at 3.5 A resolution by X-ray crystallography. The double-shelled structure consists of two different proteins, the core protein P3 and the outer shell protein P8. The atomic structure shows structural and electrostatic complementarities between both homologous (P3-P3 and P8-P8) and heterologous (P3-P8) interactions, as well as overall conformational changes found in P3-P3 dimer caused by the insertion of amino-terminal loop regions of one of the P3 protein into the other. These interactions suggest how the 900 protein components are built into a higher-ordered virus core structure. The atomic structure of rice dwarf virus reveals the self-assembly mechanism of component proteins.,Nakagawa A, Miyazaki N, Taka J, Naitow H, Ogawa A, Fujimoto Z, Mizuno H, Higashi T, Watanabe Y, Omura T, Cheng RH, Tsukihara T Structure. 2003 Oct;11(10):1227-38. PMID:14527391 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Virus coat protein

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