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==Major capsid protein P1 of the Pseudomonas phage phi6==
==Major capsid protein P1 of the Pseudomonas phage phi6==
<StructureSection load='4k7h' size='340' side='right' caption='[[4k7h]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
<StructureSection load='4k7h' size='340' side='right'caption='[[4k7h]], [[Resolution|resolution]] 3.60&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4k7h]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpph6 Bpph6]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K7H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4K7H FirstGlance]. <br>
<table><tr><td colspan='2'>[[4k7h]] is a 5 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=4K7H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4K7H FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">P1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10879 BPPH6])</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]] 3.5964&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4k7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7h OCA], [http://pdbe.org/4k7h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4k7h RCSB], [http://www.ebi.ac.uk/pdbsum/4k7h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7h 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=4k7h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4k7h OCA], [https://pdbe.org/4k7h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4k7h RCSB], [https://www.ebi.ac.uk/pdbsum/4k7h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4k7h ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://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.  
[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 ==
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>
</div>
<div class="pdbe-citations 4k7h" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Bpph6]]
[[Category: Large Structures]]
[[Category: Boura, E]]
[[Category: Pseudomonas virus phi6]]
[[Category: Hurley, J H]]
[[Category: Boura E]]
[[Category: Nemecek, D]]
[[Category: Hurley JH]]
[[Category: Plevka, P]]
[[Category: Nemecek D]]
[[Category: Steven, C A]]
[[Category: Plevka P]]
[[Category: Major capsid protein]]
[[Category: Steven CA]]
[[Category: Viral protein]]
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