View source for 4btg


==Coordinates of the bacteriophage phi6 capsid subunits (P1A and P1B) fitted into the cryoEM reconstruction of the procapsid at 4.4 A resolution==
<SX load='4btg' size='340' side='right' viewer='molstar' caption='[[4btg]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4btg]] is a 2 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=4BTG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BTG 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]] 4.4&#8491;</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=4btg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4btg OCA], [https://pdbe.org/4btg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4btg RCSB], [https://www.ebi.ac.uk/pdbsum/4btg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4btg ProSAT]</span></td></tr>
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== 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.
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== Publication Abstract from PubMed ==
The cystovirus varphi6 shares several distinct features with other double-stranded RNA (dsRNA) viruses, including the human pathogen, rotavirus: segmented genomes, nonequivalent packing of 120 subunits in its icosahedral capsid, and capsids as compartments for transcription and replication. varphi6 assembles as a dodecahedral procapsid that undergoes major conformational changes as it matures into the spherical capsid. We determined the crystal structure of the capsid protein, P1, revealing a flattened trapezoid subunit with an alpha-helical fold. We also solved the procapsid with cryo-electron microscopy to comparable resolution. Fitting the crystal structure into the procapsid disclosed substantial conformational differences between the two P1 conformers. Maturation via two intermediate states involves remodeling on a similar scale, besides huge rigid-body rotations. The capsid structure and its stepwise maturation that is coupled to sequential packaging of three RNA segments sets the cystoviruses apart from other dsRNA viruses as a dynamic molecular machine.

Subunit Folds and Maturation Pathway of a dsRNA Virus Capsid.,Nemecek D, Boura E, Wu W, Cheng N, Plevka P, Qiao J, Mindich L, Heymann JB, Hurley JH, Steven AC Structure. 2013 Aug 6;21(8):1374-83. doi: 10.1016/j.str.2013.06.007. Epub 2013, Jul 25. PMID:23891288<ref>PMID:23891288</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</SX>
[[Category: Large Structures]]
[[Category: Pseudomonas virus phi6]]
[[Category: Boura E]]
[[Category: Cheng N]]
[[Category: Heymann JB]]
[[Category: Hurley JH]]
[[Category: Mindich L]]
[[Category: Nemecek D]]
[[Category: Plevka P]]
[[Category: Qiao J]]
[[Category: Steven AC]]
[[Category: Wu W]]