View source for 5muw


==Atomic structure of P4 packaging enzyme fitted into a localized reconstruction of bacteriophage phi6 vertex==
<SX load='5muw' size='340' side='right' viewer='molstar' caption='[[5muw]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5muw]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_virus_phi6 Pseudomonas virus phi6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5MUW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MUW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5muw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muw OCA], [https://pdbe.org/5muw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5muw RCSB], [https://www.ebi.ac.uk/pdbsum/5muw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5muw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/P4_BPPH6 P4_BPPH6] P4 is one of the structural proteins of the polyhedral procapsid, which is responsible for genomic replication and transcription. Displays single-stranded RNA-stimulated NTPase activity.<ref>PMID:12239286</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Correct outer protein shell assembly is a prerequisite for virion infectivity in many multi-shelled dsRNA viruses. In the prototypic dsRNA bacteriophage phi6, the assembly reaction is promoted by calcium ions but its biomechanics remain poorly understood. Here, we describe the near-atomic resolution structure of the phi6 double-shelled particle. The outer T=13 shell protein P8 consists of two alpha-helical domains joined by a linker, which allows the trimer to adopt either a closed or an open conformation. The trimers in an open conformation swap domains with each other. Our observations allow us to propose a mechanistic model for calcium concentration regulated outer shell assembly. Furthermore, the structure provides a prime exemplar of bona fide domain-swapping. This leads us to extend the theory of domain-swapping from the level of monomeric subunits and multimers to closed spherical shells, and to hypothesize a mechanism by which closed protein shells may arise in evolution.

Double-stranded RNA virus outer shell assembly by bona fide domain-swapping.,Sun Z, El Omari K, Sun X, Ilca SL, Kotecha A, Stuart DI, Poranen MM, Huiskonen JT Nat Commun. 2017 Mar 13;8:14814. doi: 10.1038/ncomms14814. PMID:28287099<ref>PMID:28287099</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5muw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Pseudomonas virus phi6]]
[[Category: El Omari K]]
[[Category: Huiskonen JT]]
[[Category: Ilca S]]
[[Category: Kotecha A]]
[[Category: Poranen MM]]
[[Category: Stuart DI]]
[[Category: Sun X]]
[[Category: Sun Z]]