1nso

From Proteopedia

(Difference between revisions)

Current revision

Folded monomer of protease from Mason-Pfizer monkey virus

Structural highlights

1nso is a 1 chain structure with sequence from Simian retrovirus 1. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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]^[1] 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]^[2] Enhances the activity of the reverse transcriptase. May be part of the mature RT.^[3]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zabransky A, Andreansky M, Hruskova-Heidingsfeldova O, Havlicek V, Hunter E, Ruml T, Pichova I. Three active forms of aspartic proteinase from Mason-Pfizer monkey virus. Virology. 1998 Jun 5;245(2):250-6. PMID:9636364 doi:10.1006/viro.1998.9173
↑ Zabransky A, Andreansky M, Hruskova-Heidingsfeldova O, Havlicek V, Hunter E, Ruml T, Pichova I. Three active forms of aspartic proteinase from Mason-Pfizer monkey virus. Virology. 1998 Jun 5;245(2):250-6. PMID:9636364 doi:10.1006/viro.1998.9173
↑ Krizova I, Hadravova R, Stokrova J, Gunterova J, Dolezal M, Ruml T, Rumlova M, Pichova I. The G-patch domain of Mason-Pfizer monkey virus is a part of reverse transcriptase. J Virol. 2012 Feb;86(4):1988-98. doi: 10.1128/JVI.06638-11. Epub 2011 Dec 14. PMID:22171253 doi:http://dx.doi.org/10.1128/JVI.06638-11
↑ Veverka V, Bauerova H, Zabransky A, Lang J, Ruml T, Pichova I, Hrabal R. Three-dimensional structure of a monomeric form of a retroviral protease. J Mol Biol. 2003 Oct 31;333(4):771-80. PMID:14568536

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1nso"

@@ Line 1: / Line 1: @@
 ==Folded monomer of protease from Mason-Pfizer monkey virus==
-<StructureSection load='1nso' size='340' side='right' caption='[[1nso]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<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 [http://en.wikipedia.org/wiki/Srv-1 Srv-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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NSO FirstGlance]. <br>
+<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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PRT ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11942 SRV-1])</td></tr>
+</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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nso FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nso OCA], [http://pdbe.org/1nso PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1nso RCSB], [http://www.ebi.ac.uk/pdbsum/1nso PDBsum]</span></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>
+    <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>
@@ Line 29: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Srv-1]]
+[[Category: Large Structures]]
-[[Category: Bauerova, H]]
+[[Category: Simian retrovirus 1]]
-[[Category: Hrabal, R]]
+[[Category: Bauerova H]]
-[[Category: Lang, J]]
+[[Category: Hrabal R]]
-[[Category: Pichova, I]]
+[[Category: Lang J]]
-[[Category: Ruml, T]]
+[[Category: Pichova I]]
-[[Category: Veverka, V]]
+[[Category: Ruml T]]
-[[Category: Zabransky, A]]
+[[Category: Veverka V]]
-[[Category: Folded monomer]]
+[[Category: Zabransky A]]
-[[Category: Hydrolase]]
-[[Category: M-pmv]]
-[[Category: Protease]]
-[[Category: Virus maturation]]

1nso

From Proteopedia

Current revision

Folded monomer of protease from Mason-Pfizer monkey virus

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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