1o6e

From Proteopedia

Revision as of 13:39, 30 October 2007

EPSTEIN-BARR VIRUS PROTEASE

Overview

Epstein-Barr virus (EBV) belongs to the gamma-herpesvirinae subfamily of, the Herpesviridae. The protease domain of the assemblin protein of, herpesviruses forms a monomer-dimer equilibrium in solution. The protease, domain of EBV was expressed in Escherichia coli and its structure was, solved by X-ray crystallography to 2.3A resolution after inhibition with, diisopropyl-fluorophosphate (DFP). The overall structure confirms the, conservation of the homodimer and its structure throughout the alpha, beta, and gamma-herpesvirinae. The substrate recognition could be modelled, using information from the DFP binding, from a crystal contact, suggesting, that the substrate forms an antiparallel beta-strand extending strand, beta5, and from the comparison with the structure of a peptidomimetic, ... [(full description)]

About this Structure

1O6E is a [Single protein] structure of sequence from [Human herpesvirus 4] with MIP as [ligand]. Active as [Assemblin], with EC number [3.4.21.97]. Structure known Active Site: MPA. Full crystallographic information is available from [OCA].

Reference

The crystal structure of the Epstein-Barr virus protease shows rearrangement of the processed C terminus., Buisson M, Hernandez JF, Lascoux D, Schoehn G, Forest E, Arlaud G, Seigneurin JM, Ruigrok RW, Burmeister WP, J Mol Biol. 2002 Nov 15;324(1):89-103. PMID:12421561

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