3j2o: Difference between revisions

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<SX load='3j2o' size='340' side='right' viewer='molstar' caption='[[3j2o]], [[Resolution|resolution]] 25.00&Aring;' scene=''>
<SX load='3j2o' size='340' side='right' viewer='molstar' caption='[[3j2o]], [[Resolution|resolution]] 25.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3j2o]] is a 6 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=3J2O OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3J2O FirstGlance]. <br>
<table><tr><td colspan='2'>[[3j2o]] is a 6 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=3J2O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J2O FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ox3|1ox3]], [[1aa0|1aa0]], [[2bsg|2bsg]], [[3j2m|3j2m]], [[3j2n|3j2n]]</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]] 25&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">wac ([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=3j2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j2o OCA], [https://pdbe.org/3j2o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3j2o RCSB], [https://www.ebi.ac.uk/pdbsum/3j2o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3j2o 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=3j2o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j2o OCA], [http://pdbe.org/3j2o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j2o RCSB], [http://www.ebi.ac.uk/pdbsum/3j2o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j2o ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4]] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').  
[https://www.uniprot.org/uniprot/WAC_BPT4 WAC_BPT4] Chaperone responsible for attachment of long tail fibers to virus particle. Forms the fibrous structure on the neck of the virion called whiskers. During phage assembly, 6 fibritin molecules attach to each virion neck through their N-terminal domains, to form a collar with six fibers ('whiskers').
<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 3j2o" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Fibritin|Fibritin]]
*[[Fibritin|Fibritin]]
== References ==
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Bpt4]]
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Aksyuk, A A]]
[[Category: Aksyuk AA]]
[[Category: Arisaka, F]]
[[Category: Arisaka F]]
[[Category: Bowman, V D]]
[[Category: Bowman VD]]
[[Category: Fokine, A]]
[[Category: Fokine A]]
[[Category: Kanamaru, S]]
[[Category: Kanamaru S]]
[[Category: Rao, V B]]
[[Category: Rao VB]]
[[Category: Rossmann, M G]]
[[Category: Rossmann MG]]
[[Category: Zhang, Z]]
[[Category: Zhang Z]]
[[Category: Bacteriophage t4]]
[[Category: Collar whisker]]
[[Category: Fibritin]]
[[Category: Gpwac]]
[[Category: Phage neck]]
[[Category: Viral protein]]

Latest revision as of 13:09, 21 February 2024

Model of the bacteriophage T4 fibritin based on the cryo-EM reconstruction of the contracted T4 tail containing the phage collar and whiskersModel of the bacteriophage T4 fibritin based on the cryo-EM reconstruction of the contracted T4 tail containing the phage collar and whiskers

3j2o, resolution 25.00Å

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