Difference between revisions of "Part:BBa K2324005"

Revision as of 19:47, 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.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 __NOTOC__
 <partinfo>BBa_K2324005 short</partinfo>
+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.