1o6e
From Proteopedia
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{{STRUCTURE_1o6e| PDB=1o6e | SCENE= }} | {{STRUCTURE_1o6e| PDB=1o6e | SCENE= }} | ||
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===EPSTEIN-BARR VIRUS PROTEASE=== | ===EPSTEIN-BARR VIRUS PROTEASE=== | ||
+ | {{ABSTRACT_PUBMED_12421561}} | ||
- | + | ==Function== | |
- | + | [[http://www.uniprot.org/uniprot/PPR_EBVB9 PPR_EBVB9]] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein BcLF1 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as BcLF1 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein BcLF1. Cleavages products are evicted from the capsid before or during DNA packaging. Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging. Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein BcLF1. Multimerizes in the nucleus such as BcLF1 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging. | |
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==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
- | <ref group="xtra">PMID:012421561</ref><references group="xtra"/> | + | <ref group="xtra">PMID:012421561</ref><references group="xtra"/><references/> |
[[Category: Assemblin]] | [[Category: Assemblin]] | ||
[[Category: Human herpesvirus 4]] | [[Category: Human herpesvirus 4]] |
Revision as of 11:08, 16 April 2014
Contents |
EPSTEIN-BARR VIRUS PROTEASE
Template:ABSTRACT PUBMED 12421561
Function
[PPR_EBVB9] Capsid scaffolding protein acts as a scaffold protein by binding major capsid protein BcLF1 in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as BcLF1 forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and subsequently abolishes interaction with major capsid protein BcLF1. Cleavages products are evicted from the capsid before or during DNA packaging. Assemblin is a protease essential for virion assembly in the nucleus. Catalyzes the cleavage of the assembly protein after complete capsid formation. Assemblin and cleavages products are evicted from the capsid before or during DNA packaging. Assembly protein plays a major role in capsid assembly. Acts as a scaffold protein by binding major capsid protein BcLF1. Multimerizes in the nucleus such as BcLF1 forms the icosahedral T=16 capsid. Cleaved by assemblin after capsid completion. The cleavages products are evicted from the capsid before or during DNA packaging.
About this Structure
1o6e is a 2 chain structure with sequence from Human herpesvirus 4. Full crystallographic information is available from OCA.
Reference
- Buisson M, Hernandez JF, Lascoux D, Schoehn G, Forest E, Arlaud G, Seigneurin JM, Ruigrok RW, Burmeister WP. The crystal structure of the Epstein-Barr virus protease shows rearrangement of the processed C terminus. J Mol Biol. 2002 Nov 15;324(1):89-103. PMID:12421561
Categories: Assemblin | Human herpesvirus 4 | Arlaud, G. | Buisson, M. | Burmeister, W P. | Forest, E. | Hernandez, J. | Lascoux, D. | Ruigrok, R W.H. | Schoehn, G. | Seigneurin, J. | Beta-barrel | Hydrolase | Proteinase | Serine protease | Spine | Structural genomic | Structural proteomics in europe