2x53: Difference between revisions
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==Structure of the phage p2 baseplate in its activated conformation with Sr== | |||
<StructureSection load='2x53' size='340' side='right'caption='[[2x53]], [[Resolution|resolution]] 3.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2x53]] is a 27 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_virus_P2 Lactococcus virus P2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2X53 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2X53 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SR:STRONTIUM+ION'>SR</scene></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=2x53 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2x53 OCA], [https://pdbe.org/2x53 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2x53 RCSB], [https://www.ebi.ac.uk/pdbsum/2x53 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2x53 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/D3KFX5_BPLP2 D3KFX5_BPLP2] | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/x5/2x53_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2x53 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== 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<ref>PMID:20351260</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 2x53" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
< | </StructureSection> | ||
[[Category: Lactococcus | [[Category: Lactococcus virus P2]] | ||
[[Category: Bebeacua | [[Category: Large Structures]] | ||
[[Category: Bron | [[Category: Bebeacua C]] | ||
[[Category: Cambillau | [[Category: Bron P]] | ||
[[Category: Campanacci | [[Category: Cambillau C]] | ||
[[Category: Lichiere | [[Category: Campanacci V]] | ||
[[Category: Moineau | [[Category: Lichiere J]] | ||
[[Category: Ortiz-Lombardia | [[Category: Moineau S]] | ||
[[Category: Sciara | [[Category: Ortiz-Lombardia M]] | ||
[[Category: Tremblay | [[Category: Sciara G]] | ||
[[Category: | [[Category: Tremblay D]] | ||
[[Category: Van Heel M]] | |||
Latest revision as of 13:23, 20 December 2023
Structure of the phage p2 baseplate in its activated conformation with SrStructure of the phage p2 baseplate in its activated conformation with Sr
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedSiphoviridae 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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