Difference between revisions of "Part:BBa K2324005"
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The literature has shown that the terminal pili protein FimH (Le Trong et al 2010) can be modified by inserting heterologous sequences at position 225 and 258 (Pallesen et al 1995, Shembri et al 1999). However these two amino acids are in the pilin binding domain which may present difficulties when attempting to introduce large modifications. Harvard iGEM 2015 also introduced modifications at position 1 of the mature FimH protein.</p> | The literature has shown that the terminal pili protein FimH (Le Trong et al 2010) can be modified by inserting heterologous sequences at position 225 and 258 (Pallesen et al 1995, Shembri et al 1999). However these two amino acids are in the pilin binding domain which may present difficulties when attempting to introduce large modifications. Harvard iGEM 2015 also introduced modifications at position 1 of the mature FimH protein.</p> | ||
<p> | <p> | ||
| − | FimH is an the terminal protein of a bacterial type I pilus structure. As an adhesin, it binds mannose in nature. Here the FimH has been fused with a metallothionein protein domain at amino acid residue 1. This part is included in the composite part https://parts.igem.org/Part:BBa_K2324010 under the pRha promoter. </p> | + | FimH is an the terminal protein of a bacterial type I pilus structure. As an adhesin, it binds mannose in nature. Here the FimH has been fused with a metallothionein protein domain at amino acid residue 1. It is designed to be placed on the end of a type 1 pilus structure in <i> E. coli </i> with a view to binding a number of heavy metal ions. This part is included in the composite part https://parts.igem.org/Part:BBa_K2324010 under the pRha promoter. </p> |
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Revision as of 21:22, 1 November 2017
FimH+ MouseMT
The literature has shown that the terminal pili protein FimH (Le Trong et al 2010) can be modified by inserting heterologous sequences at position 225 and 258 (Pallesen et al 1995, Shembri et al 1999). However these two amino acids are in the pilin binding domain which may present difficulties when attempting to introduce large modifications. Harvard iGEM 2015 also introduced modifications at position 1 of the mature FimH protein.
FimH is an the terminal protein of a bacterial type I pilus structure. As an adhesin, it binds mannose in nature. Here the FimH has been fused with a metallothionein protein domain at amino acid residue 1. It is designed to be placed on the end of a type 1 pilus structure in E. coli with a view to binding a number of heavy metal ions. This part is included in the composite part https://parts.igem.org/Part:BBa_K2324010 under the pRha promoter.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]