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1o6e
From Proteopedia
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(New page: 200px<br /> <applet load="1o6e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1o6e, resolution 2.3Å" /> '''EPSTEIN-BARR VIRUS P...)
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Revision as of 14:51, 29 October 2007
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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 [Epstein-barr virus] with MIP as [ligand]. Active as [[1]], with EC number [3.4.21.97]. 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
Page seeded by OCA on Mon Oct 29 16:56:16 2007
Categories: Epstein-barr virus | Single protein | Arlaud, G. | Buisson, M. | Burmeister, W.P. | Forest, E. | Hernandez, J. | Lascoux, D. | Ruigrok, R.W.H. | SPINE, Structural.Proteomics.in.Europe. | Schoehn, G. | Seigneurin, J. | MIP | Assemblin | Beta-barrel | Coat protein | Domain | Hydrolase | Protease | Proteinase | Serine protease | Spine | Structural genomics | Structural proteomics in europe
