View source for 5oiy


==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 with sequence from [https://en.wikipedia.org/wiki/Human_metapneumovirus Human metapneumovirus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=5OIY 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]] 2.2&#8491;</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=5oiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5oiy OCA], [https://pdbe.org/5oiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5oiy RCSB], [https://www.ebi.ac.uk/pdbsum/5oiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5oiy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q91KZ5_9MONO Q91KZ5_9MONO] 
<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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5oiy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Human metapneumovirus]]
[[Category: Large Structures]]
[[Category: Granier S]]
[[Category: Grimes JM]]
[[Category: Grison CM]]
[[Category: Leyrat C]]
[[Category: Paesen GC]]
[[Category: Renner M]]