1zyo
From Proteopedia
(New page: 200px<br /><applet load="1zyo" size="350" color="white" frame="true" align="right" spinBox="true" caption="1zyo, resolution 2.40Å" /> '''Crystal Structure of...) |
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==Overview== | ==Overview== | ||
| - | Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal | + | Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal serine protease domain. The crystal structure of the protease domain was determined to a resolution of 2.4 A using multiple isomorphous replacement and anomalous scattering. The SeMV protease domain exhibited the characteristic trypsin fold and was found to be closer to cellular serine proteases than to other viral proteases. The residues of the S1-binding pocket, H298, T279 and N308 were mutated to alanine in the DeltaN70-Protease-VPg polyprotein, and the cis-cleavage activity was examined. The H298A and T279A mutants were inactive, while the N308A mutant was partially active, suggesting that the interactions of H298 and T279 with P1-glutamate are crucial for the E-T/S cleavage. A region of exposed aromatic amino acids, probably essential for interaction with VPg, was identified on the protease domain, and this interaction could play a major role in modulating the function of the protease. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Gayathri, P.]] | [[Category: Gayathri, P.]] | ||
| - | [[Category: Murthy, M | + | [[Category: Murthy, M R.N.]] |
[[Category: Prasad, K.]] | [[Category: Prasad, K.]] | ||
| - | [[Category: Satheshkumar, P | + | [[Category: Satheshkumar, P S.]] |
| - | [[Category: Savithri, H | + | [[Category: Savithri, H S.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: beta-barrel]] | [[Category: beta-barrel]] | ||
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[[Category: viral serine protease of trypsin fold]] | [[Category: viral serine protease of trypsin fold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:20:20 2008'' |
Revision as of 14:20, 21 February 2008
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Crystal Structure of the Serine Protease Domain of Sesbania Mosaic Virus polyprotein
Overview
Sesbania mosaic virus (SeMV) polyprotein is processed by its N-terminal serine protease domain. The crystal structure of the protease domain was determined to a resolution of 2.4 A using multiple isomorphous replacement and anomalous scattering. The SeMV protease domain exhibited the characteristic trypsin fold and was found to be closer to cellular serine proteases than to other viral proteases. The residues of the S1-binding pocket, H298, T279 and N308 were mutated to alanine in the DeltaN70-Protease-VPg polyprotein, and the cis-cleavage activity was examined. The H298A and T279A mutants were inactive, while the N308A mutant was partially active, suggesting that the interactions of H298 and T279 with P1-glutamate are crucial for the E-T/S cleavage. A region of exposed aromatic amino acids, probably essential for interaction with VPg, was identified on the protease domain, and this interaction could play a major role in modulating the function of the protease.
About this Structure
1ZYO is a Single protein structure of sequence from Sesbania mosaic virus with as ligand. Active as Glutamyl endopeptidase, with EC number 3.4.21.19 Full crystallographic information is available from OCA.
Reference
Crystal structure of the serine protease domain of Sesbania mosaic virus polyprotein and mutational analysis of residues forming the S1-binding pocket., Gayathri P, Satheshkumar PS, Prasad K, Nair S, Savithri HS, Murthy MR, Virology. 2006 Mar 15;346(2):440-51. Epub 2005 Dec 13. PMID:16356524
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