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==The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the contracted T4 tail==
==The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the contracted T4 tail==
<StructureSection load='3j2n' size='340' side='right' caption='[[3j2n]], [[Resolution|resolution]] 16.00&Aring;' scene=''>
<SX load='3j2n' size='340' side='right' viewer='molstar' caption='[[3j2n]], [[Resolution|resolution]] 16.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3j2n]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J2N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J2N FirstGlance]. <br>
<table><tr><td colspan='2'>[[3j2n]] is a 12 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T4 Escherichia virus T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J2N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J2N FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j2m|3j2m]], [[3j2o|3j2o]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 16&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">15 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4]), 18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 BPT4])</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=3j2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j2n OCA], [https://pdbe.org/3j2n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j2n RCSB], [https://www.ebi.ac.uk/pdbsum/3j2n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j2n ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j2n OCA], [http://pdbe.org/3j2n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j2n RCSB], [http://www.ebi.ac.uk/pdbsum/3j2n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j2n ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/VG15_BPT4 VG15_BPT4]] Stabilizes the tail sheath structure and produces the "connector" structure required for T4 head attachment. [[http://www.uniprot.org/uniprot/VG18_BPT4 VG18_BPT4]] The contractile tail of bacteriophage T4 consists of a contractile sheath, a tube and a baseplate. 144 protomers of Gp18, arranged in 24 annuli, form the contractile tail sheath which participates in viral DNA injection into host cytoplasm.
[https://www.uniprot.org/uniprot/COMPL_BPT4 COMPL_BPT4] Stabilizes the tail sheath structure and acts as a connector between the end of tail and the portal vertex of the capsid.<ref>PMID:23434847</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A hexamer of the bacteriophage T4 tail terminator protein, gp15, attaches to the top of the phage tail stabilizing the contractile sheath and forming the interface for binding of the independently assembled head. Here we report the crystal structure of the gp15 hexamer, describe its interactions in T4 virions that have either an extended tail or a contracted tail, and discuss its structural relationship to other phage proteins. The neck of T4 virions is decorated by the "collar" and "whiskers", made of fibritin molecules. Fibritin acts as a chaperone helping to attach the long tail fibers to the virus during the assembly process. The collar and whiskers are environment-sensing devices, regulating the retraction of the long tail fibers under unfavorable conditions, thus preventing infection. Cryo-electron microscopy analysis suggests that twelve fibritin molecules attach to the phage neck with six molecules forming the collar and six molecules forming the whiskers.
 
The Molecular Architecture of the Bacteriophage T4 Neck.,Fokine A, Zhang Z, Kanamaru S, Bowman VD, Aksyuk AA, Arisaka F, Rao VB, Rossmann MG J Mol Biol. 2013 Feb 19. pii: S0022-2836(13)00098-3. doi:, 10.1016/j.jmb.2013.02.012. PMID:23434847<ref>PMID:23434847</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3j2n" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</SX>
[[Category: Bpt4]]
[[Category: Escherichia virus T4]]
[[Category: Aksyuk, A]]
[[Category: Large Structures]]
[[Category: Arisaka, F]]
[[Category: Aksyuk A]]
[[Category: Bowman, V D]]
[[Category: Arisaka F]]
[[Category: Fokine, A]]
[[Category: Bowman VD]]
[[Category: Kanamaru, S]]
[[Category: Fokine A]]
[[Category: Rao, V B]]
[[Category: Kanamaru S]]
[[Category: Rossmann, M G]]
[[Category: Rao VB]]
[[Category: Zhang, Z]]
[[Category: Rossmann MG]]
[[Category: Bacteriophage t4]]
[[Category: Zhang Z]]
[[Category: Phage sheath protein]]
[[Category: Phage tail terminator protein]]
[[Category: Viral protein]]

Latest revision as of 13:09, 21 February 2024

The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the contracted T4 tailThe X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the contracted T4 tail

3j2n, resolution 16.00Å

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