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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 extended T4 tail== | |||
<StructureSection load='3j2m' size='340' side='right' caption='[[3j2m]], [[Resolution|resolution]] 15.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3j2m]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4 Enterobacteria phage t4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J2M OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J2M FirstGlance]. <br> | |||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j2n|3j2n]], [[3j2o|3j2o]]</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 Enterobacteria phage T4]), 18 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10665 Enterobacteria phage T4])</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=3j2m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j2m OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j2m RCSB], [http://www.ebi.ac.uk/pdbsum/3j2m PDBsum]</span></td></tr> | |||
</table> | |||
<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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Enterobacteria phage t4]] | [[Category: Enterobacteria phage t4]] | ||
[[Category: Aksyuk, A | [[Category: Aksyuk, A]] | ||
[[Category: Arisaka, F | [[Category: Arisaka, F]] | ||
[[Category: Bowman, V D | [[Category: Bowman, V D]] | ||
[[Category: Fokine, A | [[Category: Fokine, A]] | ||
[[Category: Kanamaru, S | [[Category: Kanamaru, S]] | ||
[[Category: Rao, V B | [[Category: Rao, V B]] | ||
[[Category: Rossmann, M G | [[Category: Rossmann, M G]] | ||
[[Category: Zhang, Z | [[Category: Zhang, Z]] | ||
[[Category: Bacteriophage t4]] | [[Category: Bacteriophage t4]] | ||
[[Category: Phage sheath protein]] | [[Category: Phage sheath protein]] | ||
[[Category: Phage tail terminator protein]] | [[Category: Phage tail terminator protein]] | ||
[[Category: Viral protein]] | [[Category: Viral protein]] | ||
Revision as of 18:29, 18 December 2014
The X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the extended T4 tailThe X-ray structure of the gp15 hexamer and the model of the gp18 protein fitted into the cryo-EM reconstruction of the extended T4 tail
Structural highlights
Publication Abstract from PubMedA 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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