View source for 6rao


==Cryo-EM structure of the anti-feeding prophage (AFP) baseplate, 6-fold symmetrised==
<SX load='6rao' size='340' side='right' viewer='molstar' caption='[[6rao]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6rao]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Serratia_entomophila Serratia entomophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RAO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6RAO 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]] 3.1&#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=6rao FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rao OCA], [https://pdbe.org/6rao PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6rao RCSB], [https://www.ebi.ac.uk/pdbsum/6rao PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6rao ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q6HAD8_9GAMM Q6HAD8_9GAMM] 
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== Publication Abstract from PubMed ==
Contractile injection systems are sophisticated multiprotein nanomachines that puncture target cell membranes. Although the number of atomic-resolution insights into contractile bacteriophage tails, bacterial type six secretion systems and R-pyocins is rapidly increasing, structural information on the contraction of bacterial phage-like protein-translocation structures directed towards eukaryotic hosts is scarce. Here, we characterize the antifeeding prophage AFP from Serratia entomophila by cryo-electron microscopy. We present the high-resolution structure of the entire AFP particle in the extended state, trace 11 protein chains de novo from the apical cap to the needle tip, describe localization variants and perform specific structural comparisons with related systems. We analyse inter-subunit interactions and highlight their universal conservation within contractile injection systems while revealing the specificities of AFP. Furthermore, we provide the structure of the AFP sheath-baseplate complex in a contracted state. This study reveals atomic details of interaction networks that accompany and define the contraction mechanism of toxin-delivery tailocins, offering a comprehensive framework for understanding their mode of action and for their possible adaptation as biocontrol agents.

Atomic structures of an entire contractile injection system in both the extended and contracted states.,Desfosses A, Venugopal H, Joshi T, Felix J, Jessop M, Jeong H, Hyun J, Heymann JB, Hurst MRH, Gutsche I, Mitra AK Nat Microbiol. 2019 Aug 5. pii: 10.1038/s41564-019-0530-6. doi:, 10.1038/s41564-019-0530-6. PMID:31384001<ref>PMID:31384001</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 6rao" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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[[Category: Large Structures]]
[[Category: Serratia entomophila]]
[[Category: Desfosses A]]