2bsg: Difference between revisions

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-{{Seed}}
-[[Image:2bsg.png|left|200px]]
-<!--
+==The modeled structure of fibritin (gpwac) of bacteriophage T4 based on cryo-EM reconstruction of the extended tail of bacteriophage T4==
-The line below this paragraph, containing "STRUCTURE_2bsg", creates the "Structure Box" on the page.
+<SX load='2bsg' size='340' side='right' viewer='molstar' caption='[[2bsg]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[2bsg]] is a 3 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=2BSG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BSG FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 15&#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=2bsg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bsg OCA], [https://pdbe.org/2bsg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bsg RCSB], [https://www.ebi.ac.uk/pdbsum/2bsg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bsg ProSAT]</span></td></tr>
-{{STRUCTURE_2bsg|  PDB=2bsg  |  SCENE=  }}
+</table>
+== Function ==
+[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').
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bs/2bsg_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bsg ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Bacteriophage T4 and related viruses have a contractile tail that serves as an efficient mechanical device for infecting bacteria. A three-dimensional cryo-EM reconstruction of the mature T4 tail assembly at 15-A resolution shows the hexagonal dome-shaped baseplate, the extended contractile sheath, the long tail fibers attached to the baseplate and the collar formed by six whiskers that interact with the long tail fibers. Comparison with the structure of the contracted tail shows that tail contraction is associated with a substantial rearrangement of the domains within the sheath protein and results in shortening of the sheath to about one-third of its original length. During contraction, the tail tube extends beneath the baseplate by about one-half of its total length and rotates by 345 degrees , allowing it to cross the host's periplasmic space.
-===THE MODELED STRUCTURE OF FIBRITIN (GPWAC) OF BACTERIOPHAGE T4 BASED ON CRYO-EM RECONSTRUCTION OF THE EXTENDED TAIL OF BACTERIOPHAGE T4===
+The tail structure of bacteriophage T4 and its mechanism of contraction.,Kostyuchenko VA, Chipman PR, Leiman PG, Arisaka F, Mesyanzhinov VV, Rossmann MG Nat Struct Mol Biol. 2005 Sep;12(9):810-3. Epub 2005 Aug 14. PMID:16116440<ref>PMID:16116440</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bsg" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16116440}}, adds the Publication Abstract to the page
+*[[Fibritin|Fibritin]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16116440 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16116440}}
+__TOC__
+</SX>
-==About this Structure==
+[[Category: Escherichia virus T4]]
-BSG is a 3 chains structure of sequences 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=2BSG OCA].
+[[Category: Large Structures]]
+[[Category: Arisaka F]]
-==Reference==
+[[Category: Chipman PR]]
-<ref group="xtra">PMID:16116440</ref><references group="xtra"/>
+[[Category: Kostyuchenko VA]]
-[[Category: Enterobacteria phage t4]]
+[[Category: Leiman PG]]
-[[Category: Arisaka, F.]]
+[[Category: Mesyanzhinov VV]]
-[[Category: Chipman, P R.]]
+[[Category: Rossmann MG]]
-[[Category: Kostyuchenko, V A.]]
-[[Category: Leiman, P G.]]
-[[Category: Mesyanzhinov, V V.]]
-[[Category: Rossmann, M G.]]
-[[Category: Attachment protein]]
-[[Category: Bacteriophage assembly]]
-[[Category: Bacteriophage t4]]
-[[Category: Chaperone]]
-[[Category: Coiled coil]]
-[[Category: Fibritin]]
-[[Category: Structural protein]]
-[[Category: Viral protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 14:51:46 2009''