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4v5i

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Revision as of 08:05, 29 March 2023

Structure of the Phage P2 Baseplate in its Activated Conformation with Ca

Structural highlights

4v5i is a 54 chain structure with sequence from Lactococcus virus P2. This structure supersedes the now removed PDB entries 2x54 and 2x5a. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4v5i"

@@ Line 3: / Line 3: @@
 <StructureSection load='4v5i' size='340' side='right'caption='[[4v5i]], [[Resolution|resolution]] 5.46&Aring;' scene=''>
 == 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>
+== 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;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 22: @@
 __TOC__
 </StructureSection>
-[[Category: Bplp2]]
+[[Category: Lactococcus virus P2]]
 [[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]]

4v5i

From Proteopedia

Revision as of 08:05, 29 March 2023

Structure of the Phage P2 Baseplate in its Activated Conformation with Ca

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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