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3sqf

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Crystal structure of monomeric M-PMV retroviral protease

Structural highlights

3sqf is a 2 chain structure with sequence from Mason-Pfizer monkey virus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.6324Å
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]

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 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3sqf"

@@ Line 3: / Line 3: @@
 <StructureSection load='3sqf' size='340' side='right'caption='[[3sqf]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3sqf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mpmv Mpmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SQF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3sqf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mason-Pfizer_monkey_virus Mason-Pfizer monkey virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3SQF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3SQF FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1nso|1nso]], [[3hvp|3hvp]], [[4hvp|4hvp]], [[2rsp|2rsp]], [[1yth|1yth]], [[4fiv|4fiv]], [[2fmb|2fmb]], [[3liy|3liy]], [[3nr6|3nr6]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6324&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pro, prt ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11855 MPMV])</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=3sqf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3sqf OCA], [https://pdbe.org/3sqf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3sqf RCSB], [https://www.ebi.ac.uk/pdbsum/3sqf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3sqf ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
+== Function ==
-== Publication Abstract from PubMed ==
+[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>
-Following the failure of a wide range of attempts to solve the crystal structure of M-PMV retroviral protease by molecular replacement, we challenged players of the protein folding game Foldit to produce accurate models of the protein. Remarkably, Foldit players were able to generate models of sufficient quality for successful molecular replacement and subsequent structure determination. The refined structure provides new insights for the design of antiretroviral drugs.
-Crystal structure of a monomeric retroviral protease solved by protein folding game players.,Khatib F, Dimaio F, Cooper S, Kazmierczyk M, Gilski M, Krzywda S, Zabranska H, Pichova I, Thompson J, Popovic Z, Jaskolski M, Baker D Nat Struct Mol Biol. 2011 Sep 18. doi: 10.1038/nsmb.2119. PMID:21926992<ref>PMID:21926992</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 3sqf" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 22: / Line 14: @@
 </StructureSection>
 [[Category: Large Structures]]
-[[Category: Mpmv]]
+[[Category: Mason-Pfizer monkey virus]]
-[[Category: Baker, D]]
+[[Category: Baker D]]
-[[Category: Cooper, S]]
+[[Category: Cooper S]]
-[[Category: DiMaio, F]]
+[[Category: DiMaio F]]
-[[Category: Gilski, M]]
+[[Category: Gilski M]]
-[[Category: Group, Foldit Contenders]]
+[[Category: Group Foldit Contenders]]
-[[Category: Jaskolski, M]]
+[[Category: Jaskolski M]]
-[[Category: Kazmierczyk, M]]
+[[Category: Kazmierczyk M]]
-[[Category: Khatib, F]]
+[[Category: Khatib F]]
-[[Category: Krzywda, S]]
+[[Category: Krzywda S]]
-[[Category: Pichova, I]]
+[[Category: Pichova I]]
-[[Category: Popovic, Z]]
+[[Category: Popovic Z]]
-[[Category: Thompson, J]]
+[[Category: Thompson J]]
-[[Category: Zabranska, H]]
+[[Category: Zabranska H]]
-[[Category: Aspartic protease]]
-[[Category: D-type retrovirus]]
-[[Category: Folded monomer]]
-[[Category: Hydrolase]]
-[[Category: Retropepsin]]
-[[Category: Retroviral protease]]
-[[Category: Retroviral protease folded as a monomer]]

3sqf

From Proteopedia

Current revision

Crystal structure of monomeric M-PMV retroviral protease

Structural highlights

Function

References

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