View source for 8xci


==Open state of central tail fiber of bacteriophage lambda upon binding to LamB==
<StructureSection load='8xci' size='340' side='right'caption='[[8xci]], [[Resolution|resolution]] 3.57&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8xci]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_Lambda Escherichia phage Lambda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8XCI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8XCI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.57&#8491;</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=8xci FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8xci OCA], [https://pdbe.org/8xci PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8xci RCSB], [https://www.ebi.ac.uk/pdbsum/8xci PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8xci ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TIPJ_LAMBD TIPJ_LAMBD] Attaches the virion to the host receptor LamB, inducing viral DNA ejection. During tail assembly, initiates distal tail tip assembly by interacting with gpI, gpL and gpK. During virus entry to host cell, binds strongly to host LamB in an irreversible attachment. The binding induces structural changes in the tail leading to viral DNA injection through LamB trimeric pore.<ref>PMID:6228546</ref> 
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== Publication Abstract from PubMed ==
Bacteriophage infection, a pivotal process in microbiology, initiates with the phage's tail recognizing and binding to the bacterial cell surface, which then mediates the injection of viral DNA. Although comprehensive studies on the interaction between bacteriophage lambda and its outer membrane receptor, LamB, have provided rich information about the system's biochemical properties, the precise molecular mechanism remains undetermined. This study revealed the high-resolution cryo-electron microscopy (cryo-EM) structures of the bacteriophage lambda tail complexed with its irreversible Shigella sonnei 3070 LamB receptor and the closed central tail fiber. These structures reveal the complex processes that trigger infection and demonstrate a substantial conformational change in the phage lambda tail tip upon LamB binding. Providing detailed structures of bacteriophage lambda infection initiation, this study contributes to the expanding knowledge of lambda-bacterial interaction, which holds significance in the fields of microbiology and therapeutic development.

Structural mechanism of bacteriophage lambda tail's interaction with the bacterial receptor.,Ge X, Wang J Nat Commun. 2024 May 17;15(1):4185. doi: 10.1038/s41467-024-48686-3. PMID:38760367<ref>PMID:38760367</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
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</StructureSection>
[[Category: Escherichia phage Lambda]]
[[Category: Large Structures]]
[[Category: Ge XF]]
[[Category: Wang JW]]