Difference between revisions of "Part:BBa K633001"
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<partinfo>BBa_K633001 short</partinfo>
 
<partinfo>BBa_K633001 short</partinfo>
 
EstA is an outer membrane-anchored esterase from Pseudomonas aeruginosa. An inactive EstA variant was used as an anchoring motif for the Escherichia coli cell-surface display of lipolytic enzymes.
 
EstA is an outer membrane-anchored esterase from Pseudomonas aeruginosa. An inactive EstA variant was used as an anchoring motif for the Escherichia coli cell-surface display of lipolytic enzymes.
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===Usage and Biology===
 
  
 
EstA is an autotransporter protein which consists of an N-terminal domain harboring the catalytic activity and a C-terminal domain forming a b-barrel-like structure inserted into the bacterial outer membrane which mediates the translocation of the N-terminal domain.
 
EstA is an autotransporter protein which consists of an N-terminal domain harboring the catalytic activity and a C-terminal domain forming a b-barrel-like structure inserted into the bacterial outer membrane which mediates the translocation of the N-terminal domain.
  
 
The successful cell-surface display of lipases as fusion proteins to an inactive variant of EstA has already been described in several papers, where the passenger enzymes retain their hydrolytic activities after being anchored on the outer surface of E. coli cells.
 
The successful cell-surface display of lipases as fusion proteins to an inactive variant of EstA has already been described in several papers, where the passenger enzymes retain their hydrolytic activities after being anchored on the outer surface of E. coli cells.
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===Usage and Biology===
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>

Revision as of 04:08, 17 October 2011

Linker + EstA Membrane Protein EstA is an outer membrane-anchored esterase from Pseudomonas aeruginosa. An inactive EstA variant was used as an anchoring motif for the Escherichia coli cell-surface display of lipolytic enzymes.

EstA is an autotransporter protein which consists of an N-terminal domain harboring the catalytic activity and a C-terminal domain forming a b-barrel-like structure inserted into the bacterial outer membrane which mediates the translocation of the N-terminal domain.

The successful cell-surface display of lipases as fusion proteins to an inactive variant of EstA has already been described in several papers, where the passenger enzymes retain their hydrolytic activities after being anchored on the outer surface of E. coli cells. 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 NgoMIV site found at 217
  • 1000
    COMPATIBLE WITH RFC[1000]