5iv7

From Proteopedia

(Difference between revisions)

Revision as of 18:36, 6 March 2020

Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate

5iv7, resolution 6.77Å

Structural highlights

5iv7 is a 96 chain structure with sequence from Enterobacteria phage t4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[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.^[1] ^[2] [BP08_BPT4] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.^[3] ^[4] [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]^[5] ^[6] [BP07_BPT4] Baseplate protein that is part of the baseplate wedge. Involved in the tail assembly.^[7] ^[8] [BP53_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.^[9] ^[10] [BP06_BPT4] Baseplate protein that is part of the baseplate wedge (PubMed:15315755). Involved in the tail assembly.^[11] ^[12] [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).^[13] ^[14] [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.^[15] ^[16]

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^[17]

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
↑ 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
↑ 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
↑ Watts NR, Hainfeld J, Coombs DH. Localization of the proteins gp7, gp8 and gp10 in the bacteriophage T4 baseplate with colloidal gold: F(ab)2 and undecagold: Fab' conjugates. J Mol Biol. 1990 Nov 20;216(2):315-25. PMID:2254933 doi:http://dx.doi.org/10.1016/S0022-2836(05)80323-7
↑ 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
↑ 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
↑ 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
↑ Kostyuchenko VA, Navruzbekov GA, Kurochkina LP, Strelkov SV, Mesyanzhinov VV, Rossmann MG. The structure of bacteriophage T4 gene product 9: the trigger for tail contraction. Structure. 1999 Oct 15;7(10):1213-22. PMID:10545330
↑ 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
↑ Leiman PG, Shneider MM, Mesyanzhinov VV, Rossmann MG. Evolution of bacteriophage tails: Structure of T4 gene product 10. J Mol Biol. 2006 May 5;358(3):912-21. Epub 2006 Mar 9. PMID:16554069 doi:10.1016/j.jmb.2006.02.058
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5iv7"

@@ Line 1: / Line 1: @@
-{{Large structure}}
 ==Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate==
-<StructureSection load='5iv7' size='340' side='right' caption='[[5iv7]], [[Resolution|resolution]] 6.77&Aring;' scene=''>
+<SX load='5iv7' size='340' side='right' viewer='molstar' caption='[[5iv7]], [[Resolution|resolution]] 6.77&Aring;' scene=''>
 == 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>
 </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], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5iv7 ProSAT]</span></td></tr>
 </table>
-{{Large structure}}
 == 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>
@@ Line 21: / Line 20: @@
 <references/>
 __TOC__
-</StructureSection>
+</SX>
 [[Category: Enterobacteria phage t4]]
+[[Category: Large Structures]]
 [[Category: Goldie, K N]]
 [[Category: Guerrero-Ferreira, R C]]

5iv7

From Proteopedia

Revision as of 18:36, 6 March 2020

Cryo-electron microscopy structure of the star-shaped, hubless post-attachment T4 baseplate

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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