3ts6
From Proteopedia
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- | [[Image:3ts6.png|left|200px]] | ||
- | + | ==Crystal structure of M-PMV DUTPASE relaxed end-product (dUMP) complex== | |
+ | <StructureSection load='3ts6' size='340' side='right'caption='[[3ts6]], [[Resolution|resolution]] 1.84Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3ts6]] 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=3TS6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TS6 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.84Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CSO:S-HYDROXYCYSTEINE'>CSO</scene>, <scene name='pdbligand=UMP:2-DEOXYURIDINE+5-MONOPHOSPHATE'>UMP</scene></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=3ts6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ts6 OCA], [https://pdbe.org/3ts6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ts6 RCSB], [https://www.ebi.ac.uk/pdbsum/3ts6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ts6 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> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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:016582495<ref>PMID:016582495</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 3ts6" style="background-color:#fffaf0;"></div> | |
- | + | ||
==See Also== | ==See Also== | ||
- | *[[ | + | *[[DUTPase 3D structures|DUTPase 3D structures]] |
- | + | == References == | |
- | == | + | <references/> |
- | < | + | __TOC__ |
- | [[Category: | + | </StructureSection> |
- | [[Category: | + | [[Category: Large Structures]] |
- | [[Category: Barabas | + | [[Category: Mason-Pfizer monkey virus]] |
- | [[Category: Nemeth | + | [[Category: Barabas O]] |
- | [[Category: Vertessy | + | [[Category: Nemeth V]] |
- | + | [[Category: Vertessy GB]] | |
- | + |
Current revision
Crystal structure of M-PMV DUTPASE relaxed end-product (dUMP) complex
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