Difference between revisions of "Part:BBa K257018:Design"

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===Design Notes===
 
===Design Notes===
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AIDA-I is the adhesin involved in diffuse adherence of E.coli. It belongs to the monomeric autotransporter protein family of the type-V secretion pathway. AIDA-I is synthesized from the aidA gene as a 145 kDa pre-proprotein with three domains : first, an N-terminal sec-dependent signal sequence that allows transport across the inner membrane; second, a cenral domain of 100kDa, the mature AIDA-I, bearing the functional part of the protein; and finally, a C-terminal membrane-embedded domain of 45kDa, AIDAc, which is predicted to form a pore in the outer membrane and might serve as a translocation conduit for mature AIDA-I.
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We had to deal with considerations about the linker domain which links the translocated protein to the translocator domain of AIDA-I. In fact, this linker needs to have a minimal length so that the protein translocated would be really functional at the outer side of the outer membrane.
 
We had to deal with considerations about the linker domain which links the translocated protein to the translocator domain of AIDA-I. In fact, this linker needs to have a minimal length so that the protein translocated would be really functional at the outer side of the outer membrane.
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AIDA Translocator domain has been designed using a fusion silver standard 23 prefix in order to be able to make a fusion protein with the N terminal extremity of AIDA translocator.
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AIDA Translocator domain has been designed using a fusion silver standard 23 prefix in order to be able to make a fusion protein with the N terminal extremity of AIDA translocator. The protein passenger should have both standard 23 (silver fusion) suffix and prefix to allow us to build the fusion protein as follows :
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sequence signal + passenger + aida translocator
  
 
===Source===
 
===Source===

Latest revision as of 16:46, 21 October 2009

AIDA-I autotransporter, linker + translocator domains


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 1118
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Design Notes

AIDA-I is the adhesin involved in diffuse adherence of E.coli. It belongs to the monomeric autotransporter protein family of the type-V secretion pathway. AIDA-I is synthesized from the aidA gene as a 145 kDa pre-proprotein with three domains : first, an N-terminal sec-dependent signal sequence that allows transport across the inner membrane; second, a cenral domain of 100kDa, the mature AIDA-I, bearing the functional part of the protein; and finally, a C-terminal membrane-embedded domain of 45kDa, AIDAc, which is predicted to form a pore in the outer membrane and might serve as a translocation conduit for mature AIDA-I.

We had to deal with considerations about the linker domain which links the translocated protein to the translocator domain of AIDA-I. In fact, this linker needs to have a minimal length so that the protein translocated would be really functional at the outer side of the outer membrane.

AIDA Translocator domain has been designed using a fusion silver standard 23 prefix in order to be able to make a fusion protein with the N terminal extremity of AIDA translocator. The protein passenger should have both standard 23 (silver fusion) suffix and prefix to allow us to build the fusion protein as follows : sequence signal + passenger + aida translocator

Source

AIDA has been synthesized in vitro.

References