This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2h2z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
 +
|DOMAIN=
 +
|RELATEDENTRY=
 +
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2h2z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2h2z OCA], [http://www.ebi.ac.uk/pdbsum/2h2z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2h2z RCSB]</span>
}}
}}
Line 31: Line 34:
[[Category: sar]]
[[Category: sar]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:11:59 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:24:47 2008''

Revision as of 00:24, 31 March 2008


PDB ID 2h2z

Drag the structure with the mouse to rotate
, resolution 1.6Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Crystal structure of SARS-CoV main protease with authentic N and C-termini


Overview

The viral proteases have proven to be the most selective and useful for removing the fusion tags in fusion protein expression systems. As a key enzyme in the viral life-cycle, the main protease (M(pro)) is most attractive for drug design targeting the SARS coronavirus (SARS-CoV), the etiological agent responsible for the outbreak of severe acute respiratory syndrome (SARS) in 2003. In this study, SARS-CoV M(pro) was used to specifically remove the GST tag in a new fusion protein expression system. We report a new method to produce wild-type (WT) SARS-CoV M(pro) with authentic N and C termini, and compare the activity of WT protease with those of three different types of SARS-CoV M(pro) with additional residues at the N or C terminus. Our results show that additional residues at the N terminus, but not at the C terminus, of M(pro) are detrimental to enzyme activity. To explain this, the crystal structures of WT SARS-CoV M(pro) and its complex with a Michael acceptor inhibitor were determined to 1.6 Angstroms and 1.95 Angstroms resolution respectively. These crystal structures reveal that the first residue of this protease is important for sustaining the substrate-binding pocket and inhibitor binding. This study suggests that SARS-CoV M(pro) could serve as a new tag-cleavage endopeptidase for protein overproduction, and the WT SARS-CoV M(pro) is more appropriate for mechanistic characterization and inhibitor design.

About this Structure

2H2Z is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.

Reference

Production of authentic SARS-CoV M(pro) with enhanced activity: application as a novel tag-cleavage endopeptidase for protein overproduction., Xue X, Yang H, Shen W, Zhao Q, Li J, Yang K, Chen C, Jin Y, Bartlam M, Rao Z, J Mol Biol. 2007 Feb 23;366(3):965-75. Epub 2006 Dec 1. PMID:17189639

Page seeded by OCA on Mon Mar 31 03:24:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools