2hob: Difference between revisions
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[[Image:2hob.jpg|left|200px]] | [[Image:2hob.jpg|left|200px]] | ||
'''Crystal structure of SARS-CoV main protease with authentic N and C-termini in complex with a Michael acceptor N3''' | {{Structure | ||
|PDB= 2hob |SIZE=350|CAPTION= <scene name='initialview01'>2hob</scene>, resolution 1.95Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=3IH:N-[(5-METHYLISOXAZOL-3-YL)CARBONYL]ALANYL-L-VALYL-N~1~-((1R,2Z)-4-(BENZYLOXY)-4-OXO-1-{[(3R)-2-OXOPYRROLIDIN-3-YL]METHYL}BUT-2-ENYL)-L-LEUCINAMIDE'>3IH</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''Crystal structure of SARS-CoV main protease with authentic N and C-termini in complex with a Michael acceptor N3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2HOB is a [ | 2HOB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sars_coronavirus Sars coronavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HOB OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/17189639 17189639] | ||
[[Category: Sars coronavirus]] | [[Category: Sars coronavirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sars-cov]] | [[Category: sars-cov]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:19:31 2008'' | ||
Revision as of 18:19, 20 March 2008
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Crystal structure of SARS-CoV main protease with authentic N and C-termini in complex with a Michael acceptor N3
OverviewOverview
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 StructureAbout this Structure
2HOB is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.
ReferenceReference
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
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