1nso
From Proteopedia
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| - | [[Image:1nso.gif|left|200px]] | + | [[Image:1nso.gif|left|200px]] |
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| - | '''Folded monomer of protease from Mason-Pfizer monkey virus''' | + | {{Structure |
| + | |PDB= 1nso |SIZE=350|CAPTION= <scene name='initialview01'>1nso</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= PRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39068 Simian retrovirus 2]) | ||
| + | }} | ||
| + | |||
| + | '''Folded monomer of protease from Mason-Pfizer monkey virus''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1NSO is a [ | + | 1NSO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Simian_retrovirus_2 Simian retrovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSO OCA]. |
==Reference== | ==Reference== | ||
| - | Three-dimensional structure of a monomeric form of a retroviral protease., Veverka V, Bauerova H, Zabransky A, Lang J, Ruml T, Pichova I, Hrabal R, J Mol Biol. 2003 Oct 31;333(4):771-80. PMID:[http:// | + | Three-dimensional structure of a monomeric form of a retroviral protease., Veverka V, Bauerova H, Zabransky A, Lang J, Ruml T, Pichova I, Hrabal R, J Mol Biol. 2003 Oct 31;333(4):771-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14568536 14568536] |
[[Category: Simian retrovirus 2]] | [[Category: Simian retrovirus 2]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: virus maturation]] | [[Category: virus maturation]] | ||
| - | ''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 13:01:12 2008'' |
Revision as of 11:01, 20 March 2008
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| Gene: | PRT (Simian retrovirus 2) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Folded monomer of protease from Mason-Pfizer monkey virus
Overview
The assembly of Mason-Pfizer monkey virus Gag polyproteins into immature capsids and their cleavage by the encoded protease are temporally and spatially separated processes, making the virus a particularly useful model for investigation of protease activation. Here we present a high resolution NMR structure of a fully folded monomer of a 12 kDa M-PMV protease (wt 12 PR) and of a Cys7Ala/Asp26Asn/Cys106Ala mutant (12 PR(D26N/C7A/C106A)). The overall structures of both wt 12 PR and 12 PR(D26N/C7A/C106A) follow the conservative structural motif of other retroviral proteases. The most prominent difference from the canonical fold of retroviral proteases is the absence of the interfacial beta-sheet, which leads to the loss of the principal force stabilizing the dimer of M-PMV PR. The monomer-dimer equilibrium can be shifted in favor of the dimer by adding a substrate or an inhibitor, partially compensating for the missing role of the beta-sheet. We also show that cysteines C7 and C106 play a crucial role in stabilizing the dimer and consequently increasing the proteolytic activity of M-PMV PR. This is consistent with the role of reversible oxidative modification of the cysteine residues in the regulation of the maturation of assembled M-PMV capsids in the cytoplasm.
About this Structure
1NSO is a Single protein structure of sequence from Simian retrovirus 2. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of a monomeric form of a retroviral protease., Veverka V, Bauerova H, Zabransky A, Lang J, Ruml T, Pichova I, Hrabal R, J Mol Biol. 2003 Oct 31;333(4):771-80. PMID:14568536
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