2wzp: Difference between revisions
From Proteopedia
Jump to navigationJump to search
New page: '''Unreleased structure''' The entry 2wzp is ON HOLD Authors: Sciara, G., Bebeacua, C., Bron, P., Tremblay, D., Ortiz-Lombardia, M., Lichiere, J., van Heel, M., Campanacci, V., Moineau,... |
No edit summary |
||
| (12 intermediate revisions by the same user not shown) | |||
| Line 1: | Line 1: | ||
==Structures of Lactococcal Phage p2 Baseplate Shed Light on a Novel Mechanism of Host Attachment and Activation in Siphoviridae== | |||
<StructureSection load='2wzp' size='340' side='right'caption='[[2wzp]], [[Resolution|resolution]] 2.60Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2wzp]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_virus_P2 Lactococcus virus P2] and [https://en.wikipedia.org/wiki/Lama_glama Lama glama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2WZP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2WZP 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]] 2.6Å</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=2wzp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2wzp OCA], [https://pdbe.org/2wzp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2wzp RCSB], [https://www.ebi.ac.uk/pdbsum/2wzp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2wzp 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> | |||
== 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/wz/2wzp_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=2wzp 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 2wzp" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Lactococcus virus P2]] | |||
[[Category: Lama glama]] | |||
[[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]] | |||
