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Publication Abstract from PubMed

The P9-1 protein of Rice black streaked dwarf virus accumulates in viroplasm inclusions, which are structures that appear to play an important role in viral morphogenesis and are commonly found in viruses in the family Reoviridae. Crystallographic analysis of P9-1 revealed structural features that allow the protein to form dimers via hydrophobic interactions. Each dimer had carboxy-terminal regions, resembling arms, that extended to neighboring dimers, thereby uniting sets of four dimers via lateral hydrophobic interactions to yield cylindrical octamers. The importance of these regions for the formation of viroplasm-like inclusions was confirmed by the absence of such inclusions when P9-1 was expressed without its carboxy-terminal arm. The octamers were vertically elongated cylinders, resembling the structures formed by NSP2 of rotavirus, even though there were no significant similarities between the respective primary and secondary structures of the two proteins. Our results suggest that an octameric structure with an internal pore might be important for the functioning of the respective proteins in the events that occur in the viroplasm, which might include viral morphogenesis.

Crystallographic Analysis Reveals Octamerization of Viroplasm Matrix Protein P9-1 of Rice Black Streaked Dwarf Virus.,Akita F, Higashiura A, Shimizu T, Pu Y, Suzuki M, Uehara-Ichiki T, Sasaya T, Kanamaru S, Arisaka F, Tsukihara T, Nakagawa A, Omura T J Virol. 2011 Nov 9. PMID:22072761^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.