1nso

From Proteopedia

(Difference between revisions)

Revision as of 08:52, 10 April 2024

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.

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 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 [https://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 [https://proteopedia.org/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">pol ([https://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'>[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/POL_SRV1 POL_SRV1]] Matrix protein.[UniProtKB:P07572]  Nucleocapsid protein p14: Nucleocapsid protein.[UniProtKB:P07572]  Capsid protein.[UniProtKB:P07572]  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]  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]  Enhances the activity of the reverse transcriptase. May be part of the mature RT.[UniProtKB:P07572]  RT is a multifunctional enzyme that converts the viral dimeric RNA genome into dsDNA in the cytoplasm, shortly after virus entry into the cell. This enzyme displays a DNA polymerase activity that can copy either DNA or RNA templates, and a ribonuclease H (RNase H) activity that cleaves the RNA strand of RNA-DNA heteroduplexes in a partially processive 3' to 5' endonucleasic mode. Conversion of viral genomic RNA into dsDNA requires many steps. A tRNA binds to the primer-binding site (PBS) situated at the 5' end of the viral RNA. RT uses the 3' end of the tRNA primer to perfom a short round of RNA-dependent minus-strand DNA synthesis. The reading proceeds through the U5 region and ends after the repeated (R) region which is present at both ends of viral RNA. The portion of the RNA-DNA heteroduplex is digested by the RNase H, resulting in a ssDNA product attached to the tRNA primer. This ssDNA/tRNA hybridizes with the identical R region situated at the 3' end of viral RNA. This template exchange, known as minus-strand DNA strong stop transfer, can be either intra- or intermolecular. RT uses the 3' end of this newly synthesized short ssDNA to perfom the RNA-dependent minus-strand DNA synthesis of the whole template. RNase H digests the RNA template except for a polypurine tract (PPT) situated at the 5' end of the genome. It is not clear if both polymerase and RNase H activities are simultaneous. RNase H probably can proceed both in a polymerase-dependent (RNA cut into small fragments by the same RT performing DNA synthesis) and a polymerase-independent mode (cleavage of remaining RNA fragments by free RTs). Secondly, RT performs DNA-directed plus-strand DNA synthesis using the PPT that has not been removed by RNase H as primers. PPT and tRNA primers are then removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to form a circular dsDNA intermediate. Strand displacement synthesis by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA copy of the viral genome that includes long terminal repeats (LTRs) at both ends.[PROSITE-ProRule:PRU00405]  Catalyzes viral DNA integration into the host chromosome, by performing a series of DNA cutting and joining reactions.<ref>PMID:28458055</ref>
+[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]]
@@ Line 19: / Line 19: @@
 </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.
-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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1nso" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 33: / Line 24: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Srv-1]]
+[[Category: Simian retrovirus 1]]
-[[Category: Bauerova, H]]
+[[Category: Bauerova H]]
-[[Category: Hrabal, R]]
+[[Category: Hrabal R]]
-[[Category: Lang, J]]
+[[Category: Lang J]]
-[[Category: Pichova, I]]
+[[Category: Pichova I]]
-[[Category: Ruml, T]]
+[[Category: Ruml T]]
-[[Category: Veverka, V]]
+[[Category: Veverka V]]
-[[Category: Zabransky, A]]
+[[Category: Zabransky A]]
-[[Category: Folded monomer]]
-[[Category: Hydrolase]]
-[[Category: M-pmv]]
-[[Category: Protease]]
-[[Category: Virus maturation]]

1nso

From Proteopedia

Revision as of 08:52, 10 April 2024

Folded monomer of protease from Mason-Pfizer monkey virus

Structural highlights

Function

Evolutionary Conservation

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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