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Tailspike protein
From Proteopedia
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| - | <StructureSection load=' | + | <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'> |
== Function == | == 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<ref>PMID:29500571</ref>. O-antigen polysaccharides found on the outer surface of bacteria are the natural substrates for TSP<ref>PMID:20817910</ref>. |
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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 == | ||
| - | The | + | 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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| - | </ | + | |
==3D structures of tailspike protein== | ==3D structures of tailspike protein== | ||
| - | + | [[Tailspike protein 3D structures]] | |
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== References == | == References == | ||
<references/> | <references/> | ||
| + | </StructureSection> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
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