5w5f

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<SX load='5w5f' size='340' side='right' viewer='molstar' caption='[[5w5f]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
<SX load='5w5f' size='340' side='right' viewer='molstar' caption='[[5w5f]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5w5f]] is a 18 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterobacteria_phage_t4_sensu_lato Enterobacteria phage t4 sensu lato]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W5F OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W5F FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5w5f]] is a 18 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_phage_T4 Escherichia phage T4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W5F OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5W5F FirstGlance]. <br>
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</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=5w5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w5f OCA], [http://pdbe.org/5w5f PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w5f RCSB], [http://www.ebi.ac.uk/pdbsum/5w5f PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w5f ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5w5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w5f OCA], [https://pdbe.org/5w5f PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5w5f RCSB], [https://www.ebi.ac.uk/pdbsum/5w5f PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5w5f ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/TUBE_BPT4 TUBE_BPT4]] Structural component of the bacteriophage tail which consists of a contractile sheath, a tube and a baseplate. The central cylindrical segment of the tail consists of a rigid tube, composed of multiple copies of gp19, surrounded by the outer contractile sheath assembled from gp18 subunits. During infection, contraction of the sheath drives the central tube through the host outer membrane, creating a channel for DNA ejection from the capsid into the host cell.<ref>PMID:14625682</ref>
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[https://www.uniprot.org/uniprot/TUBE_BPT4 TUBE_BPT4] Structural component of the bacteriophage tail which consists of a contractile sheath, a tube and a baseplate. The central cylindrical segment of the tail consists of a rigid tube, composed of multiple copies of gp19, surrounded by the outer contractile sheath assembled from gp18 subunits. During infection, contraction of the sheath drives the central tube through the host outer membrane, creating a channel for DNA ejection from the capsid into the host cell.<ref>PMID:14625682</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The bacteriophage T4 contractile tail (containing a tube and sheath) was the first biological assembly reconstructed in three dimensions by electron microscopy at a resolution of approximately 35 A in 1968. A single-particle reconstruction of the T4 baseplate was able to generate a 4.1 A resolution map for the first two rings of the tube using the overall baseplate for alignment. We have now reconstructed the T4 tail tube at a resolution of 3.4 A, more than a 1,000-fold increase in information content for the tube from 1968. We have used legacy software (Spider) to show that we can do better than the typical 2/3 Nyquist frequency. A reasonable map can be generated with only 1.5 electrons/A2 using the higher dose images for alignment, but increasing the dose results in a better map, consistent with other reports that electron dose does not represent the main limitation on resolution in cryo-electron microscopy.
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Refined Cryo-EM Structure of the T4 Tail Tube: Exploring the Lowest Dose Limit.,Zheng W, Wang F, Taylor NMI, Guerrero-Ferreira RC, Leiman PG, Egelman EH Structure. 2017 Jul 10. pii: S0969-2126(17)30213-7. doi:, 10.1016/j.str.2017.06.017. PMID:28757144<ref>PMID:28757144</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 5w5f" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</SX>
</SX>
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[[Category: Enterobacteria phage t4 sensu lato]]
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[[Category: Escherichia phage T4]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Egelman, E H]]
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[[Category: Egelman EH]]
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[[Category: Guerrero-Ferreira, R C]]
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[[Category: Guerrero-Ferreira RC]]
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[[Category: Leiman, P G]]
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[[Category: Leiman PG]]
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[[Category: Taylor, N M]]
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[[Category: Taylor NM]]
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[[Category: Wang, F]]
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[[Category: Wang F]]
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[[Category: Zheng, W]]
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[[Category: Zheng W]]
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[[Category: Dose limit]]
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[[Category: Helical reconstruction]]
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[[Category: T4 tail tube]]
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[[Category: Viral protein]]
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Current revision

Cryo-EM structure of the T4 tail tube

5w5f, resolution 3.40Å

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