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==Crystal structure of M-PMV dUTPASE post-inversion product (dUMP) complex==
==Crystal structure of M-PMV dUTPASE post-inversion product (dUMP) complex==
<StructureSection load='3trl' size='340' side='right' caption='[[3trl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='3trl' size='340' side='right'caption='[[3trl]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3trl]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mpmv Mpmv]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TRL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TRL FirstGlance]. <br>
<table><tr><td colspan='2'>[[3trl]] is a 1 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=3TRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TRL FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></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]] 1.8&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2d4n|2d4n]], [[2d4l|2d4l]], [[2d4m|2d4m]], [[3tp1|3tp1]], [[3tpn|3tpn]], [[3tps|3tps]], [[3tpw|3tpw]], [[3tpy|3tpy]], [[3tq3|3tq3]], [[3tq4|3tq4]], [[3tq5|3tq5]], [[3trn|3trn]], [[3ts6|3ts6]], [[3tsl|3tsl]], [[3tta|3tta]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag-pro ([http://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=3trl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trl OCA], [https://pdbe.org/3trl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3trl RCSB], [https://www.ebi.ac.uk/pdbsum/3trl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3trl ProSAT]</span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.23 3.6.1.23] </span></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=3trl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3trl OCA], [http://pdbe.org/3trl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3trl RCSB], [http://www.ebi.ac.uk/pdbsum/3trl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3trl ProSAT]</span></td></tr>
</table>
</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>  
Deoxyuridine 5'-triphosphate nucleotidohydrolase from Mason-Pfizer monkey retrovirus (M-PMV dUTPase) is a betaretroviral member of the dUTPase enzyme family. In the mature M-PMV virion, this enzyme is present as the C-terminal domain of the fusion protein nucleocapsid-dUTPase. The homotrimeric organization characteristic of dUTPases is retained in this bifunctional fusion protein. The fusion protein supposedly plays a role in adequate localization of dUTPase activity in the vicinity of nucleic acids during reverse transcription and integration. Here, the nucleocapsid-free dUTPase (48 426 Da) was cocrystallized with a dUTP substrate analogue using the hanging-drop vapour-diffusion method. The obtained crystals belong to the primitive hexagonal space group P6(3), with unit-cell parameters a = 60.6, b = 60.6, c = 63.6 angstroms, alpha = 90, beta = 90, gamma = 120 degrees. Native and PtCl4-derivative data sets were collected using synchrotron radiation to 1.75 and 2.3 angstroms, respectively. Phasing was successfully performed by isomorphous replacement combined with anomalous scattering.
 
Crystallization and preliminary X-ray studies of dUTPase from Mason-Pfizer monkey retrovirus.,Barabas O, Nemeth V, Vertessy BG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt, 4):399-401. Epub 2006 Mar 25. PMID:16582495<ref>PMID:16582495</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3trl" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Deoxyuridine 5'-triphosphate nucleotidohydrolase|Deoxyuridine 5'-triphosphate nucleotidohydrolase]]
*[[DUTPase 3D structures|DUTPase 3D structures]]
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Mpmv]]
[[Category: Large Structures]]
[[Category: DUTP diphosphatase]]
[[Category: Mason-Pfizer monkey virus]]
[[Category: Barabas, O]]
[[Category: Barabas O]]
[[Category: Nemeth, V]]
[[Category: Nemeth V]]
[[Category: Vertessy, B G]]
[[Category: Vertessy BG]]
[[Category: Hydrolase]]
[[Category: Jelly roll]]

Latest revision as of 16:37, 14 March 2024

Crystal structure of M-PMV dUTPASE post-inversion product (dUMP) complexCrystal structure of M-PMV dUTPASE post-inversion product (dUMP) complex

Structural highlights

3trl is a 1 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 1.8Å
Ligands:
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]

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ 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

3trl, resolution 1.80Å

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