2GUM

Crystal structure of the extracellular domain of glycoprotein B from Herpes Simplex Virus type I

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.10 Å
  • R-Value Free: 0.275 
  • R-Value Work: 0.248 
  • R-Value Observed: 0.248 

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This is version 1.4 of the entry. See complete history. 


Literature

Crystal structure of glycoprotein B from herpes simplex virus 1.

Heldwein, E.E., Lou, H., Bender, F.C., Cohen, G.H., Eisenberg, R.J., Harrison, S.C.

(2006) Science 313: 217-220

  • DOI: https://doi.org/10.1126/science.1126548
  • Primary Citation of Related Structures:  
    2GUM

  • 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.

    • Organizational Affiliation: 

    Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA. [email protected]


Macromolecules
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(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Glycoprotein B
A, B, C
628Human alphaherpesvirus 1 strain KOSMutation(s): 0 
Gene Names: GB, UL27
UniProt
Find proteins for P06437 (Human herpesvirus 1 (strain KOS))
Explore P06437 
Go to UniProtKB:  P06437
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP06437
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

Unit Cell:
Length ( Å )Angle ( ˚ )
a = 84.959α = 67.04
b = 100.039β = 77.99
c = 100.133γ = 70.31
Software Package:
Software NamePurpose
ADSCdata collection
DENZOdata reduction
SnBphasing
CNSrefinement
SCALEPACKdata scaling

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2006-07-25
    Type: Initial release
  • Version 1.1: 2008-05-01
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Source and taxonomy, Version format compliance
  • Version 1.3: 2017-10-18
    Changes: Refinement description
  • Version 1.4: 2024-11-06
    Changes: Data collection, Database references, Derived calculations, Structure summary