This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


3trl

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (13:37, 14 March 2024) (edit) (undo)
 
Line 3: Line 3:
<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 [https://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 [https://proteopedia.org/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" id="ligandDat"><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"><div style='overflow: auto; max-height: 3em;'>[[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]]</div></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 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11855 MPMV])</td></tr>
+
-
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/dUTP_diphosphatase dUTP diphosphatase], with EC number [https://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'>[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='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>
</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==
Line 27: Line 18:
</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Mpmv]]
+
[[Category: Mason-Pfizer monkey virus]]
-
[[Category: DUTP diphosphatase]]
+
[[Category: Barabas O]]
-
[[Category: Barabas, O]]
+
[[Category: Nemeth V]]
-
[[Category: Nemeth, V]]
+
[[Category: Vertessy BG]]
-
[[Category: Vertessy, B G]]
+
-
[[Category: Hydrolase]]
+
-
[[Category: Jelly roll]]
+

Current revision

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

PDB ID 3trl

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools