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| - | {{Large structure}}
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| | ==Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate== | | ==Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate== |
| - | <StructureSection load='5iv7' size='340' side='right' caption='[[5iv7]], [[Resolution|resolution]] 6.77Å' scene=''> | + | <SX load='5iv7' size='340' side='right' viewer='molstar' caption='[[5iv7]], [[Resolution|resolution]] 6.77Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5iv7]] is a 96 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=5IV7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5IV7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5iv7]] is a 96 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=5IV7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5IV7 FirstGlance]. <br> |
| - | </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=5iv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iv7 OCA], [http://pdbe.org/5iv7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5iv7 RCSB], [http://www.ebi.ac.uk/pdbsum/5iv7 PDBsum]</span></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]] 6.77Å</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=5iv7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5iv7 OCA], [https://pdbe.org/5iv7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5iv7 RCSB], [https://www.ebi.ac.uk/pdbsum/5iv7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5iv7 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | {{Large structure}} | |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BP11_BPT4 BP11_BPT4]] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP08_BPT4 BP08_BPT4]] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP25_BPT4 BP25_BPT4]] Baseplate protein that is part of the outer wedges of the baseplate (PubMed:15315755). Probably plays a role as a connector between the central and peripheral parts of the baseplate. Involved in the tail assembly.[UniProtKB:P51768]<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP07_BPT4 BP07_BPT4]] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.<ref>PMID:2254933</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP53_BPT4 BP53_BPT4]] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4]] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> [[http://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> [[http://www.uniprot.org/uniprot/BP10_BPT4 BP10_BPT4]] Baseplate protein that is part of the baseplate wedge and that connects the short tail fibers to the baseplate (PubMed:16554069). During infection, the baseplate undergoes a conformational change from a dome-shaped to a star-shaped structure. At this point, gp10 rotates and acts as a lever that unfolds the short tail fibers, which then interact with host cell surface receptors. Involved in the tail assembly.<ref>PMID:16554069</ref> <ref>PMID:21129200</ref> | + | [https://www.uniprot.org/uniprot/BP06_BPT4 BP06_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.<ref>PMID:15315755</ref> <ref>PMID:21129200</ref> |
| | + | <div style="background-color:#fffaf0;"> |
| | + | == Publication Abstract from PubMed == |
| | + | Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved. |
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| | + | Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680<ref>PMID:27193680</ref> |
| | + | |
| | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | + | </div> |
| | + | <div class="pdbe-citations 5iv7" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Enterobacteria phage t4]] | + | [[Category: Escherichia virus T4]] |
| - | [[Category: Goldie, K N]]
| + | [[Category: Large Structures]] |
| - | [[Category: Guerrero-Ferreira, R C]]
| + | [[Category: Goldie KN]] |
| - | [[Category: Leiman, P G]]
| + | [[Category: Guerrero-Ferreira RC]] |
| - | [[Category: Stahlberg, H]]
| + | [[Category: Leiman PG]] |
| - | [[Category: Taylor, N M.I]]
| + | [[Category: Stahlberg H]] |
| - | [[Category: Bacterial virus]]
| + | [[Category: Taylor NMI]] |
| - | [[Category: Bacteriophage]] | + | |
| - | [[Category: Baseplate]] | + | |
| - | [[Category: Cell attachment]] | + | |
| - | [[Category: Hubless]]
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| - | [[Category: Infection]]
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| - | [[Category: Membrane-piercing]]
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| - | [[Category: Post-attachment]] | + | |
| - | [[Category: Star-shaped]] | + | |
| - | [[Category: T4]] | + | |
| - | [[Category: Viral protein]]
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| Structural highlights
Function
BP06_BPT4 Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.[1] [2]
Publication Abstract from PubMed
Several systems, including contractile tail bacteriophages, the type VI secretion system and R-type pyocins, use a multiprotein tubular apparatus to attach to and penetrate host cell membranes. This macromolecular machine resembles a stretched, coiled spring (or sheath) wound around a rigid tube with a spike-shaped protein at its tip. A baseplate structure, which is arguably the most complex part of this assembly, relays the contraction signal to the sheath. Here we present the atomic structure of the approximately 6-megadalton bacteriophage T4 baseplate in its pre- and post-host attachment states and explain the events that lead to sheath contraction in atomic detail. We establish the identity and function of a minimal set of components that is conserved in all contractile injection systems and show that the triggering mechanism is universally conserved.
Structure of the T4 baseplate and its function in triggering sheath contraction.,Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Leiman PG, Chipman PR, Kostyuchenko VA, Mesyanzhinov VV, Rossmann MG. Three-dimensional rearrangement of proteins in the tail of bacteriophage T4 on infection of its host. Cell. 2004 Aug 20;118(4):419-29. PMID:15315755 doi:10.1016/j.cell.2004.07.022
- ↑ Leiman PG, Arisaka F, van Raaij MJ, Kostyuchenko VA, Aksyuk AA, Kanamaru S, Rossmann MG. Morphogenesis of the T4 tail and tail fibers. Virol J. 2010 Dec 3;7:355. doi: 10.1186/1743-422X-7-355. PMID:21129200 doi:10.1186/1743-422X-7-355
- ↑ Taylor NM, Prokhorov NS, Guerrero-Ferreira RC, Shneider MM, Browning C, Goldie KN, Stahlberg H, Leiman PG. Structure of the T4 baseplate and its function in triggering sheath contraction. Nature. 2016 May 18;533(7603):346-52. doi: 10.1038/nature17971. PMID:27193680 doi:http://dx.doi.org/10.1038/nature17971
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