View source for 2xvr


==Phage T7 empty mature head shell==
<SX load='2xvr' size='340' side='right' viewer='molstar' caption='[[2xvr]], [[Resolution|resolution]] 10.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2xvr]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T7 Escherichia phage T7]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2XVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2XVR 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]] 10.8&#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=2xvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xvr OCA], [https://pdbe.org/2xvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2xvr RCSB], [https://www.ebi.ac.uk/pdbsum/2xvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2xvr ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/CAPSA_BPT7 CAPSA_BPT7] Assembles with the minor capsid protein to form an icosahedral capsid with a T=7 symmetry, about 60 nm in diameter, and consisting of 415 capsid proteins. The major and minor capsid proteins are incorporated into the capsid in about a 90/10 ratio respectively. Once the capsid is formed, encapsidates one single copy of the viral genome.<ref>PMID:20962334</ref> 
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== Publication Abstract from PubMed ==
Maturation of dsDNA bacteriophages involves assembling the virus prohead from a limited set of structural components, followed by rearrangements required for the stability that is necessary for infecting a host under challenging environmental conditions. Here, we determine the mature capsid structure of T7 at 1 nm resolution by cryo electron microscopy, and compare it with the prohead to reveal the molecular basis of T7 shell maturation. The mature capsid presents an expanded and thinner shell, with a drastic rearrangement of the major protein monomers that increases in their interacting surfaces, in turn resulting in a new bonding lattice. The rearrangements include tilting, in-plane rotation and radial expansion of the subunits, as well as a relative bending of the A and P-domains of each subunit. The unique features of this shell transformation, which does not employ the accessory proteins, inserted domains, or molecular interactions observed in other phages, suggest a simple capsid assembling strategy that may have appeared early in the evolution of these viruses.

Molecular rearrangements involved in the capsid shell maturation of bacteriophage T7.,Ionel A, Velazquez-Muriel JA, Luque D, Cuervo A, Caston JR, Valpuesta JM, Martin-Benito J, Carrascosa JL J Biol Chem. 2010 Oct 20. PMID:20962334<ref>PMID:20962334</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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[[Category: Escherichia phage T7]]
[[Category: Large Structures]]
[[Category: Carrascosa JL]]
[[Category: Caston JR]]
[[Category: Cuervo A]]
[[Category: Ionel A]]
[[Category: Luque D]]
[[Category: Martin-Benito J]]
[[Category: Valpuesta JM]]
[[Category: Velazquez-Muriel JA]]