2gt7
From Proteopedia
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|PDB= 2gt7 |SIZE=350|CAPTION= <scene name='initialview01'>2gt7</scene>, resolution 1.82Å | |PDB= 2gt7 |SIZE=350|CAPTION= <scene name='initialview01'>2gt7</scene>, resolution 1.82Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC ACID'>MES</scene> | + | |LIGAND= <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2gt8|2GT8]], [[2gtb|2GTB]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2gt7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2gt7 OCA], [http://www.ebi.ac.uk/pdbsum/2gt7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2gt7 RCSB]</span> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Liu, J.]] | [[Category: Liu, J.]] | ||
[[Category: Powers, J C.]] | [[Category: Powers, J C.]] | ||
| - | [[Category: MES]] | ||
[[Category: 3c-like]] | [[Category: 3c-like]] | ||
[[Category: alpha-helical domain]] | [[Category: alpha-helical domain]] | ||
| Line 41: | Line 43: | ||
[[Category: specificity pocket]] | [[Category: specificity pocket]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:21:15 2008'' |
Revision as of 00:21, 31 March 2008
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| , resolution 1.82Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Related: | 2GT8, 2GTB
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structure of SARS coronavirus main peptidase at pH 6.0 in the space group P21
Overview
The SARS coronavirus main peptidase (SARS-CoV M(pro)) plays an essential role in the life-cycle of the virus and is a primary target for the development of anti-SARS agents. Here, we report the crystal structure of M(pro) at a resolution of 1.82 Angstroms, in space group P2(1) at pH 6.0. In contrast to the previously reported structure of M(pro) in the same space group at the same pH, the active sites and the S1 specificity pockets of both protomers in the structure of M(pro) reported here are in the catalytically competent conformation, suggesting their conformational flexibility. We report two crystal structures of M(pro) having an additional Ala at the N terminus of each protomer (M(+A(-1))(pro)), both at a resolution of 2.00 Angstroms, in space group P4(3)2(1)2: one unbound and one bound by a substrate-like aza-peptide epoxide (APE). In the unbound form, the active sites and the S1 specificity pockets of both protomers of M(+A(-1))(pro) are observed in a collapsed (catalytically incompetent) conformation; whereas they are in an open (catalytically competent) conformation in the APE-bound form. The observed conformational flexibility of the active sites and the S1 specificity pockets suggests that these parts of M(pro) exist in dynamic equilibrium. The structural data further suggest that the binding of APE to M(pro) follows an induced-fit model. The substrate likely also binds in an induced-fit manner in a process that may help drive the catalytic cycle.
About this Structure
2GT7 is a Single protein structure of sequence from Sars coronavirus. Full crystallographic information is available from OCA.
Reference
Crystal structures reveal an induced-fit binding of a substrate-like Aza-peptide epoxide to SARS coronavirus main peptidase., Lee TW, Cherney MM, Liu J, James KE, Powers JC, Eltis LD, James MN, J Mol Biol. 2007 Feb 23;366(3):916-32. Epub 2006 Dec 2. PMID:17196984
Page seeded by OCA on Mon Mar 31 03:21:15 2008
Categories: Sars coronavirus | Single protein | Cherney, M M. | Eltis, L D. | Huitema, C. | James, K E. | James, M N.G. | Lee, T W. | Liu, J. | Powers, J C. | 3c-like | Alpha-helical domain | Catalytic dyad | Chymotrypsin-like fold | Cysteine peptidase | Dimer | Long loop | N-finger | Specificity pocket
