5muu: Difference between revisions
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==dsRNA bacteriophage phi6 nucleocapsid== | |||
<SX load='5muu' size='340' side='right' viewer='molstar' caption='[[5muu]], [[Resolution|resolution]] 4.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5muu]] is a 13 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=5MUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5MUU 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]] 4Å</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=5muu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5muu OCA], [https://pdbe.org/5muu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5muu RCSB], [https://www.ebi.ac.uk/pdbsum/5muu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5muu ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/P1_BPPH6 P1_BPPH6] P1 is the major inner capsid (core) protein of the polyhedral procapsid, which is responsible for genomic replication and transcription. Forms a dodecahedral shell from 60 asymmetric dimers. Binds to RNA and may be involved in genomic packaging. | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5muu" 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 SL]] | |||
[[Category: Kotecha A]] | |||
[[Category: Poranen MM]] | |||
[[Category: Stuart DI]] | |||
[[Category: Sun X]] | |||
[[Category: Sun Z]] | |||
Latest revision as of 17:50, 8 November 2023
dsRNA bacteriophage phi6 nucleocapsid
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