View source for 4btp


==Structure of the capsid protein P1 of the bacteriophage phi8==
<StructureSection load='4btp' size='340' side='right'caption='[[4btp]], [[Resolution|resolution]] 3.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4btp]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_phage_phi8 Pseudomonas phage phi8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4BTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4BTP FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.7&#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=4btp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4btp OCA], [https://pdbe.org/4btp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4btp RCSB], [https://www.ebi.ac.uk/pdbsum/4btp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4btp ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q9MC13_9VIRU Q9MC13_9VIRU] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The hallmark of a virus is its capsid, which harbors the viral genome and is formed from protein subunits, which assemble following precise geometric rules. dsRNA viruses use an unusual protein multiplicity (120 copies) to form their closed capsids. We have determined the atomic structure of the capsid protein (P1) from the dsRNA cystovirus Phi8. In the crystal P1 forms pentamers, very similar in shape to facets of empty procapsids, suggesting an unexpected assembly pathway that proceeds via a pentameric intermediate. Unlike the elongated proteins used by dsRNA mammalian reoviruses, P1 has a compact trapezoid-like shape and a distinct arrangement in the shell, with two near-identical conformers in nonequivalent structural environments. Nevertheless, structural similarity with the analogous protein from the mammalian viruses suggests a common ancestor. The unusual shape of the molecule may facilitate dramatic capsid expansion during phage maturation, allowing P1 to switch interaction interfaces to provide capsid plasticity.

Plate Tectonics of Virus Shell Assembly and Reorganization in Phage Phi8, a Distant Relative of Mammalian Reoviruses.,El Omari K, Sutton G, Ravantti JJ, Zhang H, Walter TS, Grimes JM, Bamford DH, Stuart DI, Mancini EJ Structure. 2013 Jul 23. pii: S0969-2126(13)00240-2. doi:, 10.1016/j.str.2013.06.017. PMID:23891291<ref>PMID:23891291</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4btp" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Pseudomonas phage phi8]]
[[Category: Bamford DH]]
[[Category: El Omari K]]
[[Category: Grimes JM]]
[[Category: Mancini EJ]]
[[Category: Ravantti JJ]]
[[Category: Stuart DI]]
[[Category: Sutton G]]
[[Category: Walter TS]]
[[Category: Zhang H]]