2d4n: Difference between revisions
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==Crystal Structure of M-PMV dUTPase complexed with dUPNPP, substrate analogue== | ==Crystal Structure of M-PMV dUTPase complexed with dUPNPP, substrate analogue== | ||
<StructureSection load='2d4n' size='340' side='right' caption='[[2d4n]], [[Resolution|resolution]] 1.53Å' scene=''> | <StructureSection load='2d4n' size='340' side='right' caption='[[2d4n]], [[Resolution|resolution]] 1.53Å' scene=''> | ||
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<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='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='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='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=2d4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4n OCA], [http://pdbe.org/2d4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d4n RCSB], [http://www.ebi.ac.uk/pdbsum/2d4n PDBsum]</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=2d4n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4n OCA], [http://pdbe.org/2d4n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2d4n RCSB], [http://www.ebi.ac.uk/pdbsum/2d4n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2d4n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
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</div> | </div> | ||
<div class="pdbe-citations 2d4n" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 2d4n" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 15:49, 12 October 2017
Crystal Structure of M-PMV dUTPase complexed with dUPNPP, substrate analogueCrystal Structure of M-PMV dUTPase complexed with dUPNPP, substrate analogue
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe homotrimeric fusion protein nucleocapsid (NC)-dUTPase combines domains that participate in RNA/DNA folding, reverse transcription, and DNA repair in Mason-Pfizer monkey betaretrovirus infected cells. The structural organization of the fusion protein remained obscured by the N- and C-terminal flexible segments of dUTPase and the linker region connecting the two domains that are invisible in electron density maps. Small-angle X-ray scattering reveals that upon oligonucleotide binding the NC domains adopt the trimeric symmetry of dUTPase. High-resolution X-ray structures together with molecular modeling indicate that fusion with NC domains dramatically alters the conformation of the flexible C-terminus by perturbing the orientation of a critical beta-strand. Consequently, the C-terminal segment is capable of double backing upon the active site of its own monomer and stabilized by non-covalent interactions formed with the N-terminal segment. This co-folding of the dUTPase terminal segments, not observable in other homologous enzymes, is due to the presence of the fused NC domain. Structural and genomic advantages of fusing the NC domain to a shortened dUTPase in betaretroviruses and the possible physiological consequences are envisaged. Flexible segments modulate co-folding of dUTPase and nucleocapsid proteins.,Nemeth-Pongracz V, Barabas O, Fuxreiter M, Simon I, Pichova I, Rumlova M, Zabranska H, Svergun D, Petoukhov M, Harmat V, Klement E, Hunyadi-Gulyas E, Medzihradszky KF, Konya E, Vertessy BG Nucleic Acids Res. 2007;35(2):495-505. Epub 2006 Dec 14. PMID:17169987[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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