View source for 6rtl


==BACTERIOPHAGE SPP1 PROCAPSID-II PROTEIN==
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== Structural highlights ==
<table><tr><td colspan='2'>[[6rtl]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_phage_SPP1 Bacillus phage SPP1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RTL 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]] 4.2&#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=6rtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rtl OCA], [https://pdbe.org/6rtl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rtl RCSB], [https://www.ebi.ac.uk/pdbsum/6rtl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rtl ProSAT]</span></td></tr>
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== Function ==
[https://www.uniprot.org/uniprot/CAPSD_BPSPP CAPSD_BPSPP] Capsid protein self-assembles, with the help of the scaffolding protein gp11, to form an icosahedral capsid with a T=7 symmetry, about 61 nm in diameter. The capsid encapsulates the genomic DNA.<ref>PMID:10656821</ref> <ref>PMID:22514336</ref> 
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== Publication Abstract from PubMed ==
Assembly of tailed bacteriophages and herpesviruses starts with formation of procapsids (virion precursors without DNA). Scaffolding proteins (SP) drive assembly by chaperoning the major capsid protein (MCP) to build an icosahedral lattice. Here we report near-atomic resolution cryo-EM structures of the bacteriophage SPP1 procapsid, the intermediate expanded procapsid with partially released SPs, and the mature capsid with DNA. In the intermediate state, SPs are bound only to MCP pentons and to adjacent subunits from hexons. SP departure results in the expanded state associated with unfolding of the MCP N-terminus and straightening of E-loops. The newly formed extensive inter-capsomere bonding appears to compensate for release of SPs that clasp MCP capsomeres together. Subsequent DNA packaging instigates bending of MCP A domain loops outwards, closing the hexons central opening and creating the capsid auxiliary protein binding interface. These findings provide a molecular basis for the sequential structural rearrangements during viral capsid maturation.

Structural transitions during the scaffolding-driven assembly of a viral capsid.,Ignatiou A, Brasiles S, El Sadek Fadel M, Burger J, Mielke T, Topf M, Tavares P, Orlova EV Nat Commun. 2019 Oct 24;10(1):4840. doi: 10.1038/s41467-019-12790-6. PMID:31649265<ref>PMID:31649265</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: Bacillus phage SPP1]]
[[Category: Large Structures]]
[[Category: Brasiles S]]
[[Category: Buerger J]]
[[Category: El Sadek M]]
[[Category: Ignatiou A]]
[[Category: Mielke T]]
[[Category: Tavares P]]
[[Category: Topf M]]