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 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]] 2.2Å</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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 5oiy" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: | [[Category: Human metapneumovirus]] | ||
[[Category: Large Structures]] | |||
[[Category: Granier S]] | |||
[[Category: Grimes JM]] | |||
[[Category: Grison CM]] | |||
[[Category: Leyrat C]] | |||
[[Category: Paesen GC]] | |||
[[Category: Renner M]] | |||
Latest revision as of 19:51, 13 December 2023
Structure of the HMPV P oligomerization domain at 2.2 AStructure of the HMPV P oligomerization domain at 2.2 A
Structural highlights
FunctionPublication 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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