PDBsum entry 2oa5

Structural protein

PDB id: 2oa5

Contents

Protein chains

92 a.a. *

97 a.a. *

Ligands

PE5 ×2

Waters ×198

* Residue conservation analysis

PDB id:

2oa5

Name:

Structural protein

Title:

Crystal structure of orf52 from murid herpesvirus (muhv-4) (murine gammaherpesvirus 68) at 2.1 a resolution. Northeast structural genomics consortium target mhr28b.

Structure:

Hypothetical protein bqlf2. Chain: a, b. Fragment: residues 1-102. Synonym: hypothetical protein gammahv.Orf52, 52. Engineered: yes

Source:

Murid herpesvirus 4. Murine herpesvirus 68. Organism_taxid: 33708. Strain: wums. Gene: bqlf2, 52, gammahv.Orf52. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.215 R-free: 0.241

Authors:

J.Benach,Y.Chen,J.Seetharaman,H.Janjua,R.Xiao,K.Cunningham,L.-C.Ma, C.K.Ho,T.B.Acton,G.T.Montelione,J.F.Hunt,L.Tong,Northeast Structural Genomics Consortium (Nesg)

Key ref:

J.Benach et al. (2007). Structural and functional studies of the abundant tegument protein ORF52 from murine gammaherpesvirus 68. J Biol Chem, 282, 31534-31541. PubMed id: 17699518 DOI: 10.1074/jbc.M705637200

Date:

14-Dec-06 Release date: 30-Jan-07

Protein chain

P88989  (P88989_MHV68) -  52 protein from Murid herpesvirus 4

Seq: 135 a.a.

Struc: 92 a.a.*

Protein chain

P88989  (P88989_MHV68) -  52 protein from Murid herpesvirus 4

Seq: 135 a.a.

Struc: 97 a.a.

* PDB and UniProt seqs differ at 4 residue positions (black crosses)

DOI no: 10.1074/jbc.M705637200

J Biol Chem 282:31534-31541 (2007)

PubMed id: 17699518

Structural and functional studies of the abundant tegument protein ORF52 from murine gammaherpesvirus 68.

J.Benach, L.Wang, Y.Chen, C.K.Ho, S.Lee, J.Seetharaman, R.Xiao, T.B.Acton, G.T.Montelione, H.Deng, R.Sun, L.Tong.

ABSTRACT

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.

Selected figure(s)

Figure 2.
FIGURE 2. Structure of ORF52 dimer. A, schematic drawing of the ORF52 dimer. Molecule A is shown in gold, and molecule B is in cyan. B, ORF52 dimer after 90° rotation around the vertical axis from A. C, a model for the ORF52 dimer with the 1 helices splayed away from the rest of the molecules. D, conserved molecular surface features of the dimer model, created with ConSurf (43). Residues that are conserved among the herpesviruses are highlighted in blue and labeled. A-C were created with Pymol (44).

Figure 3.
FIGURE 3. An asymmetric tetramer of ORF52. A, schematic drawing of the ORF52 tetramer. One dimer is shown in gold and cyan, and other is in green and magenta. B, ORF52 tetramer after 180° rotation around the vertical axis from A. C, molecular surface of the ORF52 tetramer, in the same view as A, colored by electrostatic potentials. D, molecular surface of the ORF52 tetramer in the same view as B. E, conserved molecular surface features of the ORF52 tetramer. A, B, and E created with Pymol (44), and C and D were created with Grasp (45).

The above figures are reprinted by permission from the ASBMB: J Biol Chem (2007, 282, 31534-31541) copyright 2007.

Figures were selected by an automated process.