2GUM
Crystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I
Summary for 2GUM
| Entry DOI | 10.2210/pdb2gum/pdb |
| Descriptor | Glycoprotein B, SODIUM ION (3 entities in total) |
| Functional Keywords | envelope glycoprotein, membrane fusion, viral protein |
| Biological source | Human herpesvirus 1 |
| Cellular location | Virion membrane ; Single-pass type I membrane protein : P06437 |
| Total number of polymer chains | 3 |
| Total formula weight | 215096.52 |
| Authors | Heldwein, E.E. (deposition date: 2006-05-01, release date: 2006-07-25, Last modification date: 2024-11-06) |
| Primary citation | Heldwein, E.E.,Lou, H.,Bender, F.C.,Cohen, G.H.,Eisenberg, R.J.,Harrison, S.C. Crystal structure of glycoprotein B from herpes simplex virus 1. Science, 313:217-220, 2006 Cited by PubMed Abstract: Glycoprotein B (gB) is the most conserved component of the complex cell-entry machinery of herpes viruses. A crystal structure of the gB ectodomain from herpes simplex virus type 1 reveals a multidomain trimer with unexpected homology to glycoprotein G from vesicular stomatitis virus (VSV G). An alpha-helical coiled-coil core relates gB to class I viral membrane fusion glycoproteins; two extended beta hairpins with hydrophobic tips, homologous to fusion peptides in VSV G, relate gB to class II fusion proteins. Members of both classes accomplish fusion through a large-scale conformational change, triggered by a signal from a receptor-binding component. The domain connectivity within a gB monomer would permit such a rearrangement, including long-range translocations linked to viral and cellular membranes. PubMed: 16840698DOI: 10.1126/science.1126548 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.1 Å) |
Structure validation
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