1o6e

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1o6e.gif|left|200px]]
+
{{Seed}}
 +
[[Image:1o6e.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1o6e| PDB=1o6e | SCENE= }}
{{STRUCTURE_1o6e| PDB=1o6e | SCENE= }}
-
'''EPSTEIN-BARR VIRUS PROTEASE'''
+
===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 inhibitor bound to cytomegalovirus protease. The long insert between beta-strands 1 and 2, which was disordered in the KSHV protease structure, was found to be ordered in the EBV protease and shows the same conformation as observed for proteases in the alpha and beta-herpesvirus families. In contrast to previous structures, the long loop located between beta-strands 5 and 6 is partially ordered, probably due to DFP inhibition and a crystal contact. It also contributes to substrate recognition. The protease shows a specific recognition of its own C terminus in a binding pocket involving residue Phe210 of the other monomer interacting across the dimer interface. This suggests conformational changes of the protease domain after its release from the assemblin precursor followed by burial of the new C terminus and a possible effect onto the monomer-dimer equilibrium. The importance of the processed C terminus was confirmed using a mutant protease carrying a C-terminal extension and a mutated release site, which shows different solution properties and a strongly reduced enzymatic activity.
+
The line below this paragraph, {{ABSTRACT_PUBMED_12421561}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 12421561 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_12421561}}
==About this Structure==
==About this Structure==
Line 44: Line 48:
[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:08:05 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 15:51:47 2008''

Revision as of 12:51, 28 July 2008

Image:1o6e.png

Template:STRUCTURE 1o6e

EPSTEIN-BARR VIRUS PROTEASE

Template:ABSTRACT PUBMED 12421561

About this Structure

1O6E is a Single protein structure of sequence from Human herpesvirus 4. 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 Jul 28 15:51:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1o6e"
Personal tools