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| | <SX load='6rtl' size='340' side='right' viewer='molstar' caption='[[6rtl]], [[Resolution|resolution]] 4.20Å' scene=''> | | <SX load='6rtl' size='340' side='right' viewer='molstar' caption='[[6rtl]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6rtl]] is a 7 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpspp Bpspp]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6RTL FirstGlance]. <br> | + | <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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">13 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10724 BPSPP])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6rtl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rtl OCA], [http://pdbe.org/6rtl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rtl RCSB], [http://www.ebi.ac.uk/pdbsum/6rtl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rtl 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=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> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> | + | [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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bpspp]] | + | [[Category: Bacillus phage SPP1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Brasiles, S]] | + | [[Category: Brasiles S]] |
| - | [[Category: Buerger, J]] | + | [[Category: Buerger J]] |
| - | [[Category: Ignatiou, A]] | + | [[Category: El Sadek M]] |
| - | [[Category: Mielke, T]] | + | [[Category: Ignatiou A]] |
| - | [[Category: Sadek, M El]] | + | [[Category: Mielke T]] |
| - | [[Category: Tavares, P]] | + | [[Category: Tavares P]] |
| - | [[Category: Topf, M]] | + | [[Category: Topf M]] |
| - | [[Category: 3d reconstruction]]
| + | |
| - | [[Category: Bacteriophage]]
| + | |
| - | [[Category: Capsid protein]]
| + | |
| - | [[Category: Cryo electron microscopy]]
| + | |
| - | [[Category: Maturation process]]
| + | |
| - | [[Category: Virus]]
| + | |
| Structural highlights
Function
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.[1] [2]
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[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Droge A, Santos MA, Stiege AC, Alonso JC, Lurz R, Trautner TA, Tavares P. Shape and DNA packaging activity of bacteriophage SPP1 procapsid: protein components and interactions during assembly. J Mol Biol. 2000 Feb 11;296(1):117-32. doi: 10.1006/jmbi.1999.3450. PMID:10656821 doi:http://dx.doi.org/10.1006/jmbi.1999.3450
- ↑ White HE, Sherman MB, Brasiles S, Jacquet E, Seavers P, Tavares P, Orlova EV. Capsid structure and its stability at the late stages of bacteriophage SPP1 assembly. J Virol. 2012 Jun;86(12):6768-77. Epub 2012 Apr 18. PMID:22514336 doi:10.1128/JVI.00412-12
- ↑ Ignatiou A, Brasiles S, El Sadek Fadel M, Burger J, Mielke T, Topf M, Tavares P, Orlova EV. Structural transitions during the scaffolding-driven assembly of a viral capsid. Nat Commun. 2019 Oct 24;10(1):4840. doi: 10.1038/s41467-019-12790-6. PMID:31649265 doi:http://dx.doi.org/10.1038/s41467-019-12790-6
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