View source for 6hhk


==Structure of gp105 of Listeria bacteriophage A511==
<StructureSection load='6hhk' size='340' side='right'caption='[[6hhk]], [[Resolution|resolution]] 2.38&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hhk]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Listeria_virus_A511 Listeria virus A511]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HHK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6HHK 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]] 2.38&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</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=6hhk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hhk OCA], [https://pdbe.org/6hhk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6hhk RCSB], [https://www.ebi.ac.uk/pdbsum/6hhk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6hhk ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A8AST9_BPA51 A8AST9_BPA51] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Contractile injection systems (bacteriophage tails, type VI secretions system, R-type pyocins, etc.) utilize a rigid tube/contractile sheath assembly for breaching the envelope of bacterial and eukaryotic cells. Among contractile injection systems, bacteriophages that infect Gram-positive bacteria represent the least understood members. Here, we describe the structure of Listeria bacteriophage A511 tail in its pre- and post-host attachment states (extended and contracted, respectively) using cryo-electron microscopy, cryo-electron tomography, and X-ray crystallography. We show that the structure of the tube-baseplate complex of A511 is similar to that of phage T4, but the A511 baseplate is decorated with different receptor-binding proteins, which undergo a large structural transformation upon host attachment and switch the symmetry of the baseplate-tail fiber assembly from threefold to sixfold. For the first time under native conditions, we show that contraction of the phage tail sheath assembly starts at the baseplate and propagates through the sheath in a domino-like motion.

Structure and transformation of bacteriophage A511 baseplate and tail upon infection of Listeria cells.,Guerrero-Ferreira RC, Hupfeld M, Nazarov S, Taylor NM, Shneider MM, Obbineni JM, Loessner MJ, Ishikawa T, Klumpp J, Leiman PG EMBO J. 2019 Feb 1;38(3). pii: embj.201899455. doi: 10.15252/embj.201899455. Epub, 2019 Jan 2. PMID:30606715<ref>PMID:30606715</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hhk" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Listeria virus A511]]
[[Category: Guerrero-Ferreira RC]]
[[Category: Leiman PG]]
[[Category: Taylor NMI]]