Difference between revisions of "Part:BBa K283036"

Revision as of 17:17, 20 October 2009

invasin(1-625aa)

The invasin protein of Yersinia pseudotuberculosis has been utilized for heterologous surface display. Y. pseudotuberculosis invasin promotes bacterial entry by binding to host cell integrins. It is a 986-residue protein of which the 500 N-terminal aa are thought to reside in the outer membrane. The C-terminal 497 residues, which make up the extracellular part, are involved in the binding to integrin. Nakajima and co-workers developed a system for expression of random peptides on the cell surface of E. coli by creation of a fusion hybrid between a peptide and the invasin protein. This part can be used to display fusion protein on the surface of bacteria.

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
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 886
1000
COMPATIBLE WITH RFC[1000]

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 <partinfo>BBa_K283036 short</partinfo>
-The invasin protein of ''Yersinia pseudotuberculosis'' has been utilized for heterologous surface display. Y. pseudotuberculosis invasin promotes bacterial entry by binding to host cell integrins. It is a 986-residue protein of which the  500 N-terminal aa are thought to reside in the outer membrane. The C-terminal 497 residues, which make up the extracellular part, are involved in the binding to integrin. Nakajima and co-workers developed a system for expression of random peptides on the cell surface of E. coli by creation of a fusion hybrid between a peptide and the invasin protein. The fusion protein consists of the first 625 aa of invasin, a six aa long proline spacer, and a decamer of random peptides flanked by cysteine residues.
+The invasin protein of ''Yersinia pseudotuberculosis'' has been utilized for heterologous surface display. ''Y. pseudotuberculosis'' invasin promotes bacterial entry by binding to host cell integrins. It is a 986-residue protein of which the  500 N-terminal aa are thought to reside in the outer membrane. The C-terminal 497 residues, which make up the extracellular part, are involved in the binding to integrin. Nakajima and co-workers developed a system for expression of random peptides on the cell surface of ''E. coli'' by creation of a fusion hybrid between a peptide and the invasin protein. This part can be used to display fusion protein on the surface of bacteria.
 <!-- Add more about the biology of this part here