Difference between revisions of "Part:BBa K633001"

Revision as of 15:22, 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.


Three Dimensional Structure of the "Esta" Membrane Protein, including its esterease translocated domain.

Stefan Becker, Sebastian Theile, Nele Heppeler, Anja Michalczyk, Alexander Wentzel, Susanne Wilhelm, Karl-Erich Jaeger, Harald Kolmar, A generic system for the Escherichia coli cell-surface display of lipolytic enzymes, FEBS Letters, Volume 579, Issue 5, 14 February 2005, Pages 1177-1182, ISSN 0014-5793, 10.1016/j.febslet.2004.12.087. (http://www.sciencedirect.com/science/article/pii/S0014579305000748)
Van Den Berg, B. (2010). Crystal structure of a full-length autotransporter. Journal of Molecular Biology, 396(3), 627-633. Elsevier Ltd. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/20060837

Sequence and Features