2oa5

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spinqualitylabelsall models 2oa5, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of ORF52 from Murid herpesvirus (MUHV-4) (Murine gammaherpesvirus 68) at 2.1 A resolution. Northeast Structural Genomics Consortium target MHR28B.

Overview

The tegument is a layer of proteins between the nucleocapsid and the, envelope of herpesviruses. The functions of most tegument proteins are, still poorly understood. In murine gammaherpesvirus-68 (MHV-68), ORF52 is, an abundant tegument protein of 135 residues that is required for the, assembly and release of infectious virus particles. To help understand the, molecular basis for the function of this protein, we have determined its, crystal structure at 2.1 A resolution. The structure reveals a dimeric, association of this protein. Interestingly, an N-terminal a-helix that, assumes different conformation in the two monomers of the dimer. This, helix mediates the formation of an asymmetrical tetramer, and contains, many highly conserved residues. Structural and sequence analyses suggest, this helix is more likely involved in interactions with other components, of the tegument or nucleocapsid of the virus, and that ORF52 functions as, a symmetrical dimer. The asymmetrical tetramer of ORF52 may be a 'latent', form of the protein, when it is not involved in virion assembly. The, self-association of ORF52 has been confirmed by co-immunoprecipitation and, fluorescence resonance energy transfer experiments. Deletion of the, N-terminal a-helix, as well as mutation of the conserved Arg95 residue, abolished the function of ORF52. Results of the functional studies are, fully consistent with the structural observations, and indicate that the, N-terminal a-helix is a crucial site of interaction for ORF52.

About this Structure

2OA5 is a Single protein structure of sequence from Murid herpesvirus 1 with as ligand. Full crystallographic information is available from OCA.

Reference

Structural and functional studies of the abundant tegument protein ORF52 from murine gammaherpesvirus-68., Benach J, Wang L, Chen Y, Ho CK, Lee S, Seetharaman J, Xiao R, Acton TB, Montelione GT, Deng H, Sun R, Tong L, J Biol Chem. 2007 Aug 15;. PMID:17699518

Page seeded by OCA on Wed Jan 23 13:24:32 2008