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PMID:12574112
| Citation |
Bowman, BR, Baker, ML, Rixon, FJ, Chiu, W and Quiocho, FA (2003) Structure of the herpesvirus major capsid protein. EMBO J. 22:757-65 |
|---|---|
| Abstract |
Herpes simplex virus-1 (HSV-1) virions are large, complex enveloped particles containing a proteinaceous tegument layer connected to an icosahedral capsid. The major capsid protein, VP5 (149 kDa), makes up both types of capsomere, pentons and hexons. Limited trypsin digestion of VP5 identified a single stable 65 kDa fragment which represents a proposed protein folding nucleus. We report the 2.9 A crystal structure of this fragment and its modeling into an 8.5 A resolution electron cryomicroscopy map of the HSV-1 capsid. The structure, the first for any capsid protein from Herpesviridae, revealed a novel fold, placing herpesviruses outside any of the structurally linked viral groupings. Alterations in the geometrical arrangements of the VP5 subunits in the capsomeres exposes different residues, resulting in the differential association of the tegument and VP26 with the pentons and hexons, respectively. The rearrangements of VP5 subunits required to form both pentavalent and hexavalent capsomeres result in structures that exhibit very different electrostatic properties. These differences may mediate the binding and release of other structural proteins during capsid maturation. |
| Links |
PubMed PMC145446 Online version:10.1093/emboj/cdg086 |
| Keywords |
Capsid Proteins/chemistry; Capsid Proteins/metabolism; Cryoelectron Microscopy; Crystallography, X-Ray; Herpesvirus 1, Human/chemistry; Herpesvirus 1, Human/metabolism; Protein Structure, Tertiary |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0039622: T=16 icosahedral viral capsid |
ECO:0000314: |
C |
The authors isolate a 65kda fragment of VP5 by "limited trypsin digestion." They then identifiy this fragment as the upper domain of VP5 by x-ray crystallography. Fig 1. shows this crystalized structure of the upper domain. It identifies areas important for both interactions between VP5 proteins and interactions with other capsid proteins like VP26. The authors also identify a novel fold that is unique to the herpesvirus. |
complete | ||||
| GO:0039622: T=16 icosahedral viral capsid |
ECO:0000255: |
|
C |
Fig. 2 identifies VP5 as the major capsid protein through cryoelectron microscopy. The authors fit the crystalized structure of VP5ud (upper domain) on to a cryoelectron microscopy map of the HSV-1 capsid obtained from a publication by Zhou et al (PMID:10797014[2]). They utilize Foldhunter (PMID:11352589[1]) and the Molecular Modeling Toolkit (MMTK) to fit the x-ray structure on to the cryoelectron microscopy map of the capsid. |
complete | |||
See also
References
See Help:References for how to manage references in GONUTS.
- ↑ 1.0 1.1 Jiang, W et al. (2001) Bridging the information gap: computational tools for intermediate resolution structure interpretation. J. Mol. Biol. 308 1033-44 PubMed GONUTS page
- ↑ Zhou, ZH et al. (2000) Seeing the herpesvirus capsid at 8.5 A. Science 288 877-80 PubMed GONUTS page
