View source for 7ypx


==Cyanophage Pam3 fiber==
<StructureSection load='7ypx' size='340' side='right'caption='[[7ypx]], [[Resolution|resolution]] 3.12&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ypx]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Uncultured_cyanophage Uncultured cyanophage]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7YPX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7YPX FirstGlance]. <br>
</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=7ypx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ypx OCA], [https://pdbe.org/7ypx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ypx RCSB], [https://www.ebi.ac.uk/pdbsum/7ypx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ypx ProSAT]</span></td></tr>
</table>
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== Publication Abstract from PubMed ==
At the first step of phage infection, the receptor-binding proteins (RBPs) such as tail fibers are responsible for recognizing specific host surface receptors. The proper folding and assembly of tail fibers usually requires a chaperone encoded by the phage genome. Despite extensive studies on phage structures, the molecular mechanism of phage tail fiber assembly remains largely unknown. Here, using a minimal myocyanophage, termed Pam3, isolated from Lake Chaohu, we demonstrate that the chaperone gp25 forms a stable complex with the tail fiber gp24 at a stoichiometry of 3:3. The 3.1-A cryo-electron microscopy structure of this complex revealed an elongated structure with the gp25 trimer embracing the distal moieties of gp24 trimer at the center. Each gp24 subunit consists of three domains: the N-terminal alpha-helical domain required for docking to the baseplate, the tumor necrosis factor (TNF)-like and glycine-rich domains responsible for recognizing the host receptor. Each gp25 subunit consists of two domains: a non-conserved N-terminal beta-sandwich domain that binds to the TNF-like and glycine-rich domains of the fiber, and a C-terminal alpha-helical domain that mediates trimerization/assembly of the fiber. Structural analysis enabled us to propose the assembly mechanism of phage tail fibers, in which the chaperone first protects the intertwined and repetitive distal moiety of each fiber subunit, further ensures the proper folding of these highly plastic structural elements, and eventually enables the formation of the trimeric fiber. These findings provide the structural basis for the design and engineering of phage fibers for biotechnological applications.

Structural Insights into the Chaperone-Assisted Assembly of a Simplified Tail Fiber of the Myocyanophage Pam3.,Wei ZL, Yang F, Li B, Hou P, Kong WW, Wang J, Chen Y, Jiang YL, Zhou CZ Viruses. 2022 Oct 14;14(10). pii: v14102260. doi: 10.3390/v14102260. PMID:36298815<ref>PMID:36298815</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 7ypx" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Uncultured cyanophage]]
[[Category: Jiang YL]]
[[Category: Wei ZL]]
[[Category: Zhou CZ]]