1zku: Difference between revisions

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<SX load='1zku' size='340' side='right' viewer='molstar' caption='[[1zku]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
<SX load='1zku' size='340' side='right' viewer='molstar' caption='[[1zku]], [[Resolution|resolution]] 15.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1zku]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Bpt4 Bpt4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZKU FirstGlance]. <br>
<table><tr><td colspan='2'>[[1zku]] is a 18 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=1ZKU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZKU FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></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]] 15&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1qex|1qex]], [[1s2e|1s2e]], [[1pdl|1pdl]]</div></td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE+ETHANESULFONIC+ACID'>EPE</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">9 ([https://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=1zku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zku OCA], [https://pdbe.org/1zku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zku RCSB], [https://www.ebi.ac.uk/pdbsum/1zku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zku ProSAT]</span></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=1zku FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zku OCA], [https://pdbe.org/1zku PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1zku RCSB], [https://www.ebi.ac.uk/pdbsum/1zku PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1zku ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[https://www.uniprot.org/uniprot/VG09_BPT4 VG09_BPT4]] Structural component of the baseplate. Connects the long tail fibers to the baseplate and triggers the tail contraction after virus attachment to a host cell.  
[https://www.uniprot.org/uniprot/BP09_BPT4 BP09_BPT4] Baseplate protein that connects the long tail fibers to the baseplate and probably triggers the tail contraction after virus attachment to a host cell (PubMed:10545330). Involved in the tail assembly (PubMed:21129200).<ref>PMID:10545330</ref> <ref>PMID:21129200</ref>
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1zku ConSurf].
</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=1zku ConSurf].
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== 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 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 1zku" style="background-color:#fffaf0;"></div>
== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
[[Category: Bpt4]]
[[Category: Escherichia virus T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Kostyuchenko, V A]]
[[Category: Kostyuchenko VA]]
[[Category: Structural protein]]
[[Category: Viral protein]]

Latest revision as of 12:05, 14 February 2024

Fitting of the gp9 structure in the EM density of bacteriophage T4 extended tailFitting of the gp9 structure in the EM density of bacteriophage T4 extended tail

1zku, resolution 15.00Å

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