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1nso
From Proteopedia
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| - | [[Image:1nso.gif|left|200px]]<br /><applet load="1nso" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1nso" /> | ||
| - | '''Folded monomer of protease from Mason-Pfizer monkey virus'''<br /> | ||
| - | == | + | ==Folded monomer of protease from Mason-Pfizer monkey virus== |
| + | <StructureSection load='1nso' size='340' side='right'caption='[[1nso]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1nso]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Simian_retrovirus_1 Simian retrovirus 1]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NSO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NSO FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1nso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nso OCA], [https://pdbe.org/1nso PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1nso RCSB], [https://www.ebi.ac.uk/pdbsum/1nso PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1nso ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/PRO_MPMV PRO_MPMV] Matrix protein. Nucleocapsid protein p14: Nucleocapsid protein. Capsid protein. The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.[PROSITE-ProRule:PRU00275]<ref>PMID:9636364</ref> The aspartyl protease mediates proteolytic cleavages of Gag and Gag-Pol polyproteins during or shortly after the release of the virion from the plasma membrane. Cleavages take place as an ordered, step-wise cascade to yield mature proteins. This process is called maturation. Displays maximal activity during the budding process just prior to particle release from the cell.[PROSITE-ProRule:PRU00275]<ref>PMID:9636364</ref> Enhances the activity of the reverse transcriptase. May be part of the mature RT.<ref>PMID:22171253</ref> | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ns/1nso_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1nso ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
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. | 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. | ||
| - | + | 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<ref>PMID:14568536</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | [[Category: | + | <div class="pdbe-citations 1nso" style="background-color:#fffaf0;"></div> |
| - | [[Category: | + | == References == |
| - | [[Category: Bauerova | + | <references/> |
| - | [[Category: Hrabal | + | __TOC__ |
| - | [[Category: Lang | + | </StructureSection> |
| - | [[Category: Pichova | + | [[Category: Large Structures]] |
| - | [[Category: Ruml | + | [[Category: Simian retrovirus 1]] |
| - | [[Category: Veverka | + | [[Category: Bauerova H]] |
| - | [[Category: Zabransky | + | [[Category: Hrabal R]] |
| - | + | [[Category: Lang J]] | |
| - | + | [[Category: Pichova I]] | |
| - | + | [[Category: Ruml T]] | |
| - | + | [[Category: Veverka V]] | |
| - | + | [[Category: Zabransky A]] | |
| - | + | ||
Current revision
Folded monomer of protease from Mason-Pfizer monkey virus
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Categories: Large Structures | Simian retrovirus 1 | Bauerova H | Hrabal R | Lang J | Pichova I | Ruml T | Veverka V | Zabransky A
