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| | <SX load='1w8x' size='340' side='right' viewer='molstar' caption='[[1w8x]], [[Resolution|resolution]] 4.20Å' scene=''> | | <SX load='1w8x' size='340' side='right' viewer='molstar' caption='[[1w8x]], [[Resolution|resolution]] 4.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1w8x]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_prd1 Enterobacteria phage prd1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W8X FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1w8x]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacteria_phage_PRD1 Enterobacteria phage PRD1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W8X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1W8X FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1cjd|1cjd]], [[1gw7|1gw7]], [[1gw8|1gw8]], [[1hb5|1hb5]], [[1hb7|1hb7]], [[1hb9|1hb9]], [[1hqn|1hqn]], [[1hx6|1hx6]]</div></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]] 4.2Å</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=1w8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w8x OCA], [https://pdbe.org/1w8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w8x RCSB], [https://www.ebi.ac.uk/pdbsum/1w8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w8x 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=1w8x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1w8x OCA], [https://pdbe.org/1w8x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1w8x RCSB], [https://www.ebi.ac.uk/pdbsum/1w8x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1w8x ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/VP16_BPPRD VP16_BPPRD]] protein of the infection vertex complex, which increases the vertex stability. Anchors the vertex structure to the viral membrane. Essential for viral infectivity.<ref>PMID:15331712</ref> [[https://www.uniprot.org/uniprot/CAPSD_BPPRD CAPSD_BPPRD]] Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins. [[https://www.uniprot.org/uniprot/VP31_BPPRD VP31_BPPRD]] In association with P2 and trimeric P5, forms the spike complexes located at the 5-fold vertices of the capsid. Essential for viral infectivity. [[https://www.uniprot.org/uniprot/VP30_BPPRD VP30_BPPRD]] Minor capsid protein essential for stable capsid assembly of complete particles.<ref>PMID:11697904</ref>
| + | [https://www.uniprot.org/uniprot/CAPSD_BPPRD CAPSD_BPPRD] Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins. |
| | <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: Enterobacteria phage prd1]] | + | [[Category: Enterobacteria phage PRD1]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abrescia, N G.A]] | + | [[Category: Abrescia NGA]] |
| - | [[Category: Bamford, D H]] | + | [[Category: Bamford DH]] |
| - | [[Category: Bamford, J K.H]] | + | [[Category: Bamford JKH]] |
| - | [[Category: Burnett, R M]] | + | [[Category: Burnett RM]] |
| - | [[Category: Butcher, S J]] | + | [[Category: Butcher SJ]] |
| - | [[Category: Cockburn, J J.B]] | + | [[Category: Cockburn JJB]] |
| - | [[Category: Diprose, J M]] | + | [[Category: Diprose JM]] |
| - | [[Category: Fuller, S D]] | + | [[Category: Fuller SD]] |
| - | [[Category: Grimes, J M]] | + | [[Category: Grimes JM]] |
| - | [[Category: Martin, C San]] | + | [[Category: San Martin C]] |
| - | [[Category: Stuart, D I]] | + | [[Category: Stuart DI]] |
| - | [[Category: Sutton, G C]] | + | [[Category: Sutton GC]] |
| - | [[Category: Icosahedral virus]]
| + | |
| - | [[Category: P16 membrane protein]]
| + | |
| - | [[Category: P3 major capsid protein]]
| + | |
| - | [[Category: P30 tape measure]]
| + | |
| - | [[Category: P31 penton protein]]
| + | |
| - | [[Category: Virus]]
| + | |
| - | [[Category: Virus/viral protein]]
| + | |
| Structural highlights
Function
CAPSD_BPPRD Major capsid protein self-assembles to form an icosahedral capsid with a pseudo T=25 symmetry, about 66 nm in diameter, and consisting of 240 capsid proteins trimers. The capsid encapsulates an inner membrane and the genomic dsDNA genome. The major coat protein P3 and two assembly factors (P10 and P17) are needed during the assembly of the virus particle inside the host cell, when the capsid protein multimers are capable of enclosing the host-derived membrane, containing the virus-encoded membrane-associated proteins.
Publication Abstract from PubMed
The structure of the membrane-containing bacteriophage PRD1 has been determined by X-ray crystallography at about 4 A resolution. Here we describe the structure and location of proteins P3, P16, P30 and P31. Different structural proteins seem to have specialist roles in controlling virus assembly. The linearly extended P30 appears to nucleate the formation of the icosahedral facets (composed of trimers of the major capsid protein, P3) and acts as a molecular tape-measure, defining the size of the virus and cementing the facets together. Pentamers of P31 form the vertex base, interlocking with subunits of P3 and interacting with the membrane protein P16. The architectural similarities with adenovirus and one of the largest known virus particles PBCV-1 support the notion that the mechanism of assembly of PRD1 is scaleable and applies across the major viral lineage formed by these viruses.
Insights into assembly from structural analysis of bacteriophage PRD1.,Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martin C, Burnett RM, Stuart DI, Bamford DH, Bamford JK Nature. 2004 Nov 4;432(7013):68-74. PMID:15525981[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Abrescia NG, Cockburn JJ, Grimes JM, Sutton GC, Diprose JM, Butcher SJ, Fuller SD, San Martin C, Burnett RM, Stuart DI, Bamford DH, Bamford JK. Insights into assembly from structural analysis of bacteriophage PRD1. Nature. 2004 Nov 4;432(7013):68-74. PMID:15525981 doi:10.1038/nature03056
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