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| - | <StructureSection load='1stp' size='340' side='right' caption='Caption for this structure' scene=''> | + | <StructureSection load='3th0' size='340' side='right' caption='Glycosylated tailspike protein from bacteriophage P222 complex with octasaccharide (PDB code [[3th0]])' scene='84/841073/Cv/1'> |
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| | == Function == | | == Function == |
| | | | |
| - | '''Tailspike protein''' (TSP) of bacteriophage P22 is a trimeric protein which serves as the receptor-binding protein of the bacteriophage to its bacterial host<ref>PMID:29500571</ref>. | + | The '''tailspike protein''' (TSP) of bacteriophage is a trimeric protein which serves as the receptor-binding protein of the bacteriophage to its bacterial host<ref>PMID:29500571</ref>. O-antigen polysaccharides found on the outer surface of bacteria are the natural substrates for TSP<ref>PMID:20817910</ref>. |
| - | | + | |
| - | == Disease ==
| + | |
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| | == Relevance == | | == Relevance == |
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| | + | Bacteriophage research is becoming important due to the problem of antibiotics resistance. TSP binding to pathogenic bacteria can be used for their detection<ref>PMID:30111705</ref>. |
| | | | |
| | == Structural highlights == | | == Structural highlights == |
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| - | The N-terminal domain (NTD) (residues 1-108) of TSP is responsible for the attachment | + | The C-terminal domain (CTD) (residues 109-end) of TSP is responsible for the attachment of the tailspike protein to the O-antigen moiety on bacterial cell surface. The 3D structure of an <scene name='84/841073/Cv/3'>octasaccharide</scene> bound to CTP of TSP shows <scene name='84/841073/Cv/7'>numerous hydrophobic interactions as well as defined water molecules forming hydrogen bonds to the antigen</scene><ref>PMID:23292517</ref>. |
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| - | </StructureSection> | + | |
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| | ==3D structures of tailspike protein== | | ==3D structures of tailspike protein== |
| - | | + | [[Tailspike protein 3D structures]] |
| - | [[2xc1]] - P22TSP - bacteriophage P22<br /> | + | |
| - | [[1lkt]] - P22TSP NTD<br />
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| - | [[2vky]] - P22TSP NTD/isoleucine zipper<br />
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| - | [[2vnl]] - P22TSP NTD/isoleucine zipper (mutant)<br />
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| - | [[1tyv]], [[1tyu]], [[1tyx]], [[1tyw]], [[2vfm]], [[1tsp]] - P22TSP CTD <br />
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| - | [[1qq1]], [[1qrc]], [[1qrb]], [[2vfp]], [[2vfo]], [[2vfq]], [[1qa3]], [[1qa2]], [[1qa1]], [[2vfn]], [[1clw]] - P22TSP CTD 109-667 (mutant)<br />
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| - | [[3th0]] - P22TSP CTD + octasaccharide<br />
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| - | [[2vji]] - HK620TSP NTD - bacteriophage HK620<br />
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| - | [[2x85]], [[2vjj]], [[2x6x]] - HK520TSP CTD + hexasaccharide<br />
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| - | [[2vbe]] - TSP CTD - bacteriophage SFVI<br />
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| - | [[2vbk]] - SF6TSP CTD - bacteriophage SF6<br />
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| - | [[2vbm]] - SF6TSP CTD + tetrasaccharide<br />
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| | | | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | + | </StructureSection> |
| | + | [[Category:Topic Page]] |
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Function
The tailspike protein (TSP) of bacteriophage is a trimeric protein which serves as the receptor-binding protein of the bacteriophage to its bacterial host[1]. O-antigen polysaccharides found on the outer surface of bacteria are the natural substrates for TSP[2].
Relevance
Bacteriophage research is becoming important due to the problem of antibiotics resistance. TSP binding to pathogenic bacteria can be used for their detection[3].
Structural highlights
The C-terminal domain (CTD) (residues 109-end) of TSP is responsible for the attachment of the tailspike protein to the O-antigen moiety on bacterial cell surface. The 3D structure of an bound to CTP of TSP shows [4].
3D structures of tailspike protein
Tailspike protein 3D structures
References
- ↑ Williams J, Venkatesan K, Ayariga JA, Jackson D, Wu H, Villafane R. A genetic analysis of an important hydrophobic interaction at the P22 tailspike protein N-terminal domain. Arch Virol. 2018 Jun;163(6):1623-1633. doi: 10.1007/s00705-018-3777-y. Epub 2018 , Mar 2. PMID:29500571 doi:http://dx.doi.org/10.1007/s00705-018-3777-y
- ↑ Andres D, Hanke C, Baxa U, Seul A, Barbirz S, Seckler R. Tailspike interactions with lipopolysaccharide effect DNA ejection from phage P22 particles in vitro. J Biol Chem. 2010 Nov 19;285(47):36768-75. doi: 10.1074/jbc.M110.169003. Epub, 2010 Sep 3. PMID:20817910 doi:http://dx.doi.org/10.1074/jbc.M110.169003
- ↑ Kunstmann S, Scheidt T, Buchwald S, Helm A, Mulard LA, Fruth A, Barbirz S. Bacteriophage Sf6 Tailspike Protein for Detection of Shigella flexneri Pathogens. Viruses. 2018 Aug 15;10(8). pii: v10080431. doi: 10.3390/v10080431. PMID:30111705 doi:http://dx.doi.org/10.3390/v10080431
- ↑ Andres D, Gohlke U, Broeker NK, Schulze S, Rabsch W, Heinemann U, Barbirz S, Seckler R. An essential serotype recognition pocket on phage P22 tailspike protein forces Salmonella enterica serovar Paratyphi A O-antigen fragments to bind as nonsolution conformers. Glycobiology. 2013 Apr;23(4):486-94. doi: 10.1093/glycob/cws224. Epub 2013 Jan 3. PMID:23292517 doi:http://dx.doi.org/10.1093/glycob/cws224
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