1o6e

From Proteopedia

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Template:STRUCTURE 1o6e

Contents 1 EPSTEIN-BARR VIRUS PROTEASE 2 Function 3 About this Structure 4 Reference

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