5muu

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'''Unreleased structure'''
 
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The entry 5muu is ON HOLD until Paper Publication
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==dsRNA bacteriophage phi6 nucleocapsid==
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<SX load='5muu' size='340' side='right' viewer='molstar' caption='[[5muu]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
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== Structural highlights ==
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<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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4&#8491;</td></tr>
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<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>
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</table>
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== Function ==
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors:
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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>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 5muu" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</SX>
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[[Category: Large Structures]]
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[[Category: Pseudomonas virus phi6]]
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[[Category: El Omari K]]
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[[Category: Huiskonen JT]]
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[[Category: Ilca SL]]
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[[Category: Kotecha A]]
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[[Category: Poranen MM]]
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[[Category: Stuart DI]]
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[[Category: Sun X]]
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[[Category: Sun Z]]

Current revision

dsRNA bacteriophage phi6 nucleocapsid

5muu, resolution 4.00Å

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OCA

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