5oiy: Difference between revisions

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-'''Unreleased structure'''
-The entry 5oiy is ON HOLD
+==Structure of the HMPV P oligomerization domain at 2.2 A==
+<StructureSection load='5oiy' size='340' side='right' caption='[[5oiy]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5oiy]] is a 8 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5OIY OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5OIY FirstGlance]. <br>
+</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=5oiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oiy OCA], [http://pdbe.org/5oiy PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5oiy RCSB], [http://www.ebi.ac.uk/pdbsum/5oiy PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5oiy ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The phosphoprotein (P) is the main and essential cofactor of the RNA polymerase (L) of non-segmented, negative-strand RNA viruses. P positions the viral polymerase onto its nucleoprotein-RNA template and acts as a chaperone of the nucleoprotein (N), thereby preventing nonspecific encapsidation of cellular RNAs. The phosphoprotein of human metapneumovirus (HMPV) forms homotetramers composed of a stable oligomerization domain (Pcore) flanked by large intrinsically disordered regions (IDRs). Here we combined x-ray crystallography of Pcore with small angle x-ray scattering (SAXS)-based ensemble modeling of the full-length P protein and several of its fragments to provide a structural description of P that captures its dynamic character, and highlights the presence of varyingly stable structural elements within the IDRs. We discuss the implications of the structural properties of HMPV P for the assembly and functioning of the viral transcription/replication machinery.
-Authors: Renner, M., Paesen, G.C., Grison, C.M., Granier, S., Grimes, J.M., Leyrat, C.
+Structural dissection of human metapneumovirus phosphoprotein using small angle x-ray scattering.,Renner M, Paesen GC, Grison CM, Granier S, Grimes JM, Leyrat C Sci Rep. 2017 Nov 1;7(1):14865. doi: 10.1038/s41598-017-14448-z. PMID:29093501<ref>PMID:29093501</ref>
-Description: Structure of the HMPV P oligomerization domain at 2.2 A
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 5oiy" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Granier, S]]
+[[Category: Grimes, J M]]
+[[Category: Grison, C M]]
+[[Category: Leyrat, C]]
+[[Category: Paesen, G C]]
 [[Category: Renner, M]]
-[[Category: Leyrat, C]]
+[[Category: Mononegavirale]]
-[[Category: Paesen, G.C]]
+[[Category: P protein]]
-[[Category: Grimes, J.M]]
+[[Category: Phosphoprotein]]
-[[Category: Grison, C.M]]
+[[Category: Tetramerization]]
-[[Category: Granier, S]]
+[[Category: Viral protein]]
+[[Category: Viral replication]]