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| | <StructureSection load='5ngj' size='340' side='right'caption='[[5ngj]], [[Resolution|resolution]] 2.20Å' scene=''> | | <StructureSection load='5ngj' size='340' side='right'caption='[[5ngj]], [[Resolution|resolution]] 2.20Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5ngj]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bpt5 Bpt5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NGJ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5NGJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5ngj]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_virus_T5 Escherichia virus T5]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NGJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NGJ FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N4, ORF134, T5.145, T5p141 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10726 BPT5])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></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=5ngj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ngj OCA], [http://pdbe.org/5ngj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ngj RCSB], [http://www.ebi.ac.uk/pdbsum/5ngj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ngj 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=5ngj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ngj OCA], [https://pdbe.org/5ngj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ngj RCSB], [https://www.ebi.ac.uk/pdbsum/5ngj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ngj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TUBE_BPT5 TUBE_BPT5]] Polymerizes to make up the central tail tube that is surrounded by the tail sheath protein (TSP). Tail tube protein polymerization takes place around the tape measure protein (TMP) and is probably directed by chaperone proteins. The tail is a stack of 40 trimeric rings of the TTP. Upon binding to host cell, the tail sheath contracts and the tail tube penetrates the host envelope. The tail tube is involved in viral genome delivery during ejection.<ref>PMID:16876823</ref> <ref>PMID:24198424</ref> | + | [https://www.uniprot.org/uniprot/TUBE_BPT5 TUBE_BPT5] Polymerizes to make up the central tail tube that is surrounded by the tail sheath protein (TSP). Tail tube protein polymerization takes place around the tape measure protein (TMP) and is probably directed by chaperone proteins. The tail is a stack of 40 trimeric rings of the TTP. Upon binding to host cell, the tail sheath contracts and the tail tube penetrates the host envelope. The tail tube is involved in viral genome delivery during ejection.<ref>PMID:16876823</ref> <ref>PMID:24198424</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bpt5]] | + | [[Category: Escherichia virus T5]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Arnaud, C A]] | + | [[Category: Arnaud C-A]] |
| - | [[Category: Bacia, M]] | + | [[Category: Bacia M]] |
| - | [[Category: Boulanger, P]] | + | [[Category: Boulanger P]] |
| - | [[Category: Breyton, C]] | + | [[Category: Breyton C]] |
| - | [[Category: Effantin, G]] | + | [[Category: Effantin G]] |
| - | [[Category: Engilberge, S]] | + | [[Category: Engilberge S]] |
| - | [[Category: Girard, E]] | + | [[Category: Girard E]] |
| - | [[Category: Schoehn, G]] | + | [[Category: Schoehn G]] |
| - | [[Category: Vives, C]] | + | [[Category: Vives C]] |
| - | [[Category: Bacteriophage]]
| + | |
| - | [[Category: Tube protein]]
| + | |
| - | [[Category: Viral protein]]
| + | |
| - | [[Category: Virion protein]]
| + | |
| Structural highlights
Function
TUBE_BPT5 Polymerizes to make up the central tail tube that is surrounded by the tail sheath protein (TSP). Tail tube protein polymerization takes place around the tape measure protein (TMP) and is probably directed by chaperone proteins. The tail is a stack of 40 trimeric rings of the TTP. Upon binding to host cell, the tail sheath contracts and the tail tube penetrates the host envelope. The tail tube is involved in viral genome delivery during ejection.[1] [2]
Publication Abstract from PubMed
The vast majority of phages, bacterial viruses, possess a tail ensuring host recognition, cell wall perforation and safe viral DNA transfer from the capsid to the host cytoplasm. Long flexible tails are formed from the tail tube protein (TTP) polymerised as hexameric rings around and stacked along the tape measure protein (TMP). Here, we report the crystal structure of T5 TTP pb6 at 2.2 A resolution. Pb6 is unusual in forming a trimeric ring, although structure analysis reveals homology with all classical TTPs and related tube proteins of bacterial puncturing devices (type VI secretion system and R-pyocin). Structures of T5 tail tubes before and after interaction with the host receptor were determined by cryo-electron microscopy at 6 A resolution. Comparison of these two structures reveals that host-binding information is not propagated to the capsid through conformational changes in the tail tube, suggesting a role of the TMP in this information transduction process.
Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection.,Arnaud CA, Effantin G, Vives C, Engilberge S, Bacia M, Boulanger P, Girard E, Schoehn G, Breyton C Nat Commun. 2017 Dec 5;8(1):1953. doi: 10.1038/s41467-017-02049-3. PMID:29209037[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Effantin G, Boulanger P, Neumann E, Letellier L, Conway JF. Bacteriophage T5 structure reveals similarities with HK97 and T4 suggesting evolutionary relationships. J Mol Biol. 2006 Sep 1;361(5):993-1002. Epub 2006 Jul 31. PMID:16876823 doi:http://dx.doi.org/10.1016/j.jmb.2006.06.081
- ↑ Zivanovic Y, Confalonieri F, Ponchon L, Lurz R, Chami M, Flayhan A, Renouard M, Huet A, Decottignies P, Davidson AR, Breyton C, Boulanger P. Insights into bacteriophage T5 structure from analysis of its morphogenesis genes and protein components. J Virol. 2014 Jan;88(2):1162-74. doi: 10.1128/JVI.02262-13. Epub 2013 Nov 6. PMID:24198424 doi:http://dx.doi.org/10.1128/JVI.02262-13
- ↑ Arnaud CA, Effantin G, Vives C, Engilberge S, Bacia M, Boulanger P, Girard E, Schoehn G, Breyton C. Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection. Nat Commun. 2017 Dec 5;8(1):1953. doi: 10.1038/s41467-017-02049-3. PMID:29209037 doi:http://dx.doi.org/10.1038/s41467-017-02049-3
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