2x53
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2x53 is ON HOLD until sometime in the future Authors: Sciara, G., Bebeacua, C., Bron, P., Tremblay, D., Ortiz-Lombardia, M., Lichiere, J., vanHeel, ...) |
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| - | '''Unreleased structure''' | ||
| - | + | ==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 virus P2]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bebeacua C]] | ||
| + | [[Category: Bron P]] | ||
| + | [[Category: Cambillau C]] | ||
| + | [[Category: Campanacci V]] | ||
| + | [[Category: Lichiere J]] | ||
| + | [[Category: Moineau S]] | ||
| + | [[Category: Ortiz-Lombardia M]] | ||
| + | [[Category: Sciara G]] | ||
| + | [[Category: Tremblay D]] | ||
| + | [[Category: Van Heel M]] | ||
Current revision
Structure of the phage p2 baseplate in its activated conformation with Sr
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