5oiy: Difference between revisions
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The | ==Structure of the HMPV P oligomerization domain at 2.2 A== | ||
<StructureSection load='5oiy' size='340' side='right' caption='[[5oiy]], [[Resolution|resolution]] 2.20Å' 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. | |||
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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </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: Renner, M]] | ||
[[Category: | [[Category: Mononegavirale]] | ||
[[Category: | [[Category: P protein]] | ||
[[Category: | [[Category: Phosphoprotein]] | ||
[[Category: | [[Category: Tetramerization]] | ||
[[Category: | [[Category: Viral protein]] | ||
[[Category: Viral replication]] | |||
Revision as of 10:29, 15 November 2017
Structure of the HMPV P oligomerization domain at 2.2 AStructure of the HMPV P oligomerization domain at 2.2 A
Structural highlights
Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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