4eij: Difference between revisions

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4eij]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mumps_orthorubulavirus Mumps orthorubulavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EIJ FirstGlance]. <br>
<table><tr><td colspan='2'>[[4eij]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mumps_orthorubulavirus Mumps orthorubulavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EIJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EIJ FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2001&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=4eij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eij OCA], [https://pdbe.org/4eij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eij RCSB], [https://www.ebi.ac.uk/pdbsum/4eij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eij ProSAT]</span></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=4eij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eij OCA], [https://pdbe.org/4eij PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eij RCSB], [https://www.ebi.ac.uk/pdbsum/4eij PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eij ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/Q8QY72_9MONO Q8QY72_9MONO]] Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.[ARBA:ARBA00002047]
[https://www.uniprot.org/uniprot/Q8QY72_9MONO Q8QY72_9MONO] Essential component of the RNA polymerase and the nascent chain assembly complex. Also required during RNA synthesis.[ARBA:ARBA00002047]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The phosphoprotein (P) is virally encoded by the Rhabdoviridae and Paramyxoviridae in the order Mononegavirales. P is a self-associated oligomer and forms complexes with the large viral polymerase protein (L), the nucleocapsid protein (N), and the assembled nucleocapsid. P from different viruses has shown structural diversities even though their essential functions are the same. We systematically mapped the domains in mumps virus (MuV) P and investigated their interactions with nucleocapsid-like particles (NLPs). Similar to other P proteins, MuV P contains N-terminal, central, and C-terminal domains with flexible linkers between neighboring domains. By pulldown assays, we discovered that in addition to the previously proposed nucleocapsid binding domain (residues 343-391), the N-terminal region of MuV P (residues 1-194) could also bind NLP. Further analysis of binding kinetics was conducted using surface plasmon resonance. This is the first observation that both the N- and C-terminal regions of a negative strand RNA virus P are involved in binding the nucleocapsid. Additionally, we defined the oligomerization domain (POD) of MuV P as residues 213-277 and determined its crystal structure. The tetrameric MuV POD is formed by one pair of long parallel alpha-helices with another pair in opposite orientation. Unlike the parallel orientation of each alpha-helix in the tetramer of Sendai virus POD, this represents a novel orientation of a POD where both the N- and C-terminal domains are at either end of the tetramer. This is consistent with the observation that both the N- and C-terminal domains are involved in binding the nucleocapsid.
 
Structural and Functional Characterization of the Mumps Virus Phosphoprotein.,Cox R, Green TJ, Purushotham S, Deivanayagam C, Bedwell GJ, Prevelige PE, Luo M J Virol. 2013 May 1. PMID:23637399<ref>PMID:23637399</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4eij" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
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