4BOM
Structure of herpesvirus fusion glycoprotein B-bilayer complex revealing the protein-membrane and lateral protein-protein interaction
Summary for 4BOM
| Entry DOI | 10.2210/pdb4bom/pdb |
| EMDB information | 2380 |
| Descriptor | ENVELOPE GLYCOPROTEIN B (1 entity in total) |
| Functional Keywords | viral protein, membrane proximal region, protein coat, pseudo-atomic virus-host interaction |
| Biological source | HUMAN HERPESVIRUS 1 (HUMAN HERPES SIMPLEX VIRUS 1) |
| Total number of polymer chains | 3 |
| Total formula weight | 213377.06 |
| Authors | Maurer, U.E.,Zeev-Ben-Mordehai, Z.,Pandurangan, A.P.,Cairns, T.M.,Hannah, B.P.,Whitbeck, J.C.,Eisenberg, R.J.,Cohen, G.H.,Topf, M.,Huiskonen, J.T.,Grunewald, K. (deposition date: 2013-05-21, release date: 2013-07-31, Last modification date: 2024-05-08) |
| Primary citation | Maurer, U.E.,Zeev-Ben-Mordehai, T.,Pandurangan, A.P.,Cairns, T.M.,Hannah, B.P.,Whitbeck, J.C.,Eisenberg, R.J.,Cohen, G.H.,Topf, M.,Huiskonen, J.T.,Grunewald, K. The structure of herpesvirus fusion glycoprotein B-bilayer complex reveals the protein-membrane and lateral protein-protein interaction. Structure, 21:1396-1405, 2013 Cited by PubMed Abstract: Glycoprotein B (gB) is a key component of the complex herpesvirus fusion machinery. We studied membrane interaction of two gB ectodomain forms and present an electron cryotomography structure of the gB-bilayer complex. The two forms differed in presence or absence of the membrane proximal region (MPR) but showed an overall similar trimeric shape. The presence of the MPR impeded interaction with liposomes. In contrast, the MPR-lacking form interacted efficiently with liposomes. Lateral interaction resulted in coat formation on the membranes. The structure revealed that interaction of gB with membranes was mediated by the fusion loops and limited to the outer membrane leaflet. The observed intrinsic propensity of gB to cluster on membranes indicates an additional role of gB in driving the fusion process forward beyond the transient fusion pore opening and subsequently leading to fusion pore expansion. PubMed: 23850455DOI: 10.1016/j.str.2013.05.018 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (27 Å) |
Structure validation
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