2oa5
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The tegument is a layer of proteins between the nucleocapsid and the | + | 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, 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 alpha-helix that assumes different conformation in the two monomers of the dimer mediates the formation of an asymmetrical tetramer and contains many highly conserved residues. Structural and sequence analyses suggest that 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 alpha-helix, as well as mutation of the conserved Arg(95) residue, abolished the function of ORF52. The results of the functional studies are fully consistent with the structural observations and indicate that the N-terminal alpha-helix is a crucial site of interaction for ORF52. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Structural and functional studies of the abundant tegument protein ORF52 from murine gammaherpesvirus | + | 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 Oct 26;282(43):31534-41. Epub 2007 Aug 15. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17699518 17699518] |
[[Category: Murid herpesvirus 1]] | [[Category: Murid herpesvirus 1]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Acton, T | + | [[Category: Acton, T B.]] |
[[Category: Benach, J.]] | [[Category: Benach, J.]] | ||
[[Category: Chen, Y.]] | [[Category: Chen, Y.]] | ||
[[Category: Cunningham, K.]] | [[Category: Cunningham, K.]] | ||
| - | [[Category: Ho, C | + | [[Category: Ho, C K.]] |
| - | [[Category: Hunt, J | + | [[Category: Hunt, J F.]] |
[[Category: Janjua, H.]] | [[Category: Janjua, H.]] | ||
| - | [[Category: Ma, L | + | [[Category: Ma, L C.]] |
| - | [[Category: Montelione, G | + | [[Category: Montelione, G T.]] |
| - | [[Category: NESG, Northeast | + | [[Category: NESG, Northeast Structural Genomics Consortium.]] |
[[Category: Seetharaman, J.]] | [[Category: Seetharaman, J.]] | ||
[[Category: Tong, L.]] | [[Category: Tong, L.]] | ||
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[[Category: structural protein]] | [[Category: structural protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:16:09 2008'' |
Revision as of 16:16, 21 February 2008
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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, 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 alpha-helix that assumes different conformation in the two monomers of the dimer mediates the formation of an asymmetrical tetramer and contains many highly conserved residues. Structural and sequence analyses suggest that 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 alpha-helix, as well as mutation of the conserved Arg(95) residue, abolished the function of ORF52. The results of the functional studies are fully consistent with the structural observations and indicate that the N-terminal alpha-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. Known structural/functional Sites: and . 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 Oct 26;282(43):31534-41. Epub 2007 Aug 15. PMID:17699518
Page seeded by OCA on Thu Feb 21 18:16:09 2008
Categories: Murid herpesvirus 1 | Single protein | Acton, T B. | Benach, J. | Chen, Y. | Cunningham, K. | Ho, C K. | Hunt, J F. | Janjua, H. | Ma, L C. | Montelione, G T. | NESG, Northeast Structural Genomics Consortium. | Seetharaman, J. | Tong, L. | Xiao, R. | PE5 | Mhr28b | Nesg | Northeast structural genomics consortium | Protein structure initiative | Psi-2 | Structural genomics | Structural protein
