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| | <StructureSection load='4v5i' size='340' side='right'caption='[[4v5i]], [[Resolution|resolution]] 5.46Å' scene=''> | | <StructureSection load='4v5i' size='340' side='right'caption='[[4v5i]], [[Resolution|resolution]] 5.46Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4v5i]] is a 54 chain structure with sequence from [http://en.wikipedia.org/wiki/Bplp2 Bplp2]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2x54 2x54] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2x5a 2x5a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V5I OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4V5I FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4v5i]] is a 54 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_virus_P2 Lactococcus virus P2]. This structure supersedes the now removed PDB entries [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2x54 2x54] and [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2x5a 2x5a]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4V5I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4V5I FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2x53|2x53]], [[2wzp|2wzp]]</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=4v5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v5i OCA], [https://pdbe.org/4v5i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4v5i RCSB], [https://www.ebi.ac.uk/pdbsum/4v5i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4v5i ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4v5i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4v5i OCA], [http://pdbe.org/4v5i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4v5i RCSB], [http://www.ebi.ac.uk/pdbsum/4v5i PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4v5i ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/RBP_BPLP2 RBP_BPLP2] Binds to the host phosphopolysaccharides at the onset of infection. Upon activation by calcium, the receptor binding proteins change their conformation, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA ejection.<ref>PMID:20351260</ref> <ref>PMID:24027307</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__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bplp2]] | + | [[Category: Lactococcus virus P2]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Bebeacua, C]] | + | [[Category: Bebeacua C]] |
| - | [[Category: Bron, P]] | + | [[Category: Bron P]] |
| - | [[Category: Cambillau, C]] | + | [[Category: Cambillau C]] |
| - | [[Category: Campanacci, V]] | + | [[Category: Campanacci V]] |
| - | [[Category: Heel, M van]]
| + | [[Category: Lichiere J]] |
| - | [[Category: Lichiere, J]] | + | [[Category: Moineau S]] |
| - | [[Category: Moineau, S]] | + | [[Category: Ortiz-Lombardia M]] |
| - | [[Category: Ortiz-Lombardia, M]] | + | [[Category: Sciara G]] |
| - | [[Category: Sciara, G]] | + | [[Category: Tremblay D]] |
| - | [[Category: Tremblay, D]] | + | [[Category: Van Heel M]] |
| - | [[Category: Lactococcus lacti]] | + | |
| - | [[Category: Siphoviridae]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| Structural highlights
Function
RBP_BPLP2 Binds to the host phosphopolysaccharides at the onset of infection. Upon activation by calcium, the receptor binding proteins change their conformation, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA ejection.[1] [2]
Publication Abstract from PubMed
Siphoviridae is the most abundant viral family on earth which infects bacteria as well as archaea. All known siphophages infecting gram+ Lactococcus lactis possess a baseplate at the tip of their tail involved in host recognition and attachment. Here, we report analysis of the p2 phage baseplate structure by X-ray crystallography and electron microscopy and propose a mechanism for the baseplate activation during attachment to the host cell. This approximately 1 MDa, Escherichia coli-expressed baseplate is composed of three protein species, including six trimers of the receptor-binding protein (RBP). RBPs host-recognition domains point upwards, towards the capsid, in agreement with the electron-microscopy map of the free virion. In the presence of Ca(2+), a cation mandatory for infection, the RBPs rotated 200 degrees downwards, presenting their binding sites to the host, and a channel opens at the bottom of the baseplate for DNA passage. These conformational changes reveal a novel siphophage activation and host-recognition mechanism leading ultimately to DNA ejection.
Structure of lactococcal phage p2 baseplate and its mechanism of activation.,Sciara G, Bebeacua C, Bron P, Tremblay D, Ortiz-Lombardia M, Lichiere J, van Heel M, Campanacci V, Moineau S, Cambillau C Proc Natl Acad Sci U S A. 2010 Mar 29. PMID:20351260[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sciara G, Bebeacua C, Bron P, Tremblay D, Ortiz-Lombardia M, Lichiere J, van Heel M, Campanacci V, Moineau S, Cambillau C. Structure of lactococcal phage p2 baseplate and its mechanism of activation. Proc Natl Acad Sci U S A. 2010 Mar 29. PMID:20351260
- ↑ Bebeacua C, Tremblay D, Farenc C, Chapot-Chartier MP, Sadovskaya I, van Heel M, Veesler D, Moineau S, Cambillau C. Structure, adsorption to host, and infection mechanism of virulent lactococcal phage p2. J Virol. 2013 Nov;87(22):12302-12. PMID:24027307 doi:10.1128/JVI.02033-13
- ↑ Sciara G, Bebeacua C, Bron P, Tremblay D, Ortiz-Lombardia M, Lichiere J, van Heel M, Campanacci V, Moineau S, Cambillau C. Structure of lactococcal phage p2 baseplate and its mechanism of activation. Proc Natl Acad Sci U S A. 2010 Mar 29. PMID:20351260
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