Difference between revisions of "Part:BBa J58105"

Revision as of 10:37, 29 October 2006

Synthetic periplasmic binding protein that docks a vanillin molecule

This part corresponds to the coding sequence of a computationally engineered protein designed by Pablo Tortosa and Alfonso Jaramillo at the [http://www.enseignement.polytechnique.fr/profs/biochimie/Alfonso.Jaramillo/ Synthetic Biology group at the Ecole Polytechnique (France)]. This protein is based on a ribose-binding protein template and has been designed to stabilize its closed conformation after binding a vanillin molecule. The closed conformation is able to bind a Trg protein. This part can be used to engineer a sensor genetic device if used with the part BBa_J58104 (which implements a synthetic two-component signal transduction pathway based on a Trg-EnvZ fusion protein). This device would use phosphorylated OmpR as output.

This receptor protein has been designed computationally using a ribose binding protein as a scaffold and finding the necessary mutations to change its ligand affinity towards a vanillin molecule making E. Coli tasting flavors.

Part of the active site of the computationally designed vanillin-binding protein. Dashed lines denote h-bonds. Only the residues making h-bonds with the vanillin molecule are shown on top.

By Valencia iGEM 2006

A. Aparici (2), MC. Aroca (2), J. Carrera (1), C. Edo (1,2), G. Fuertes (2), D. Jimenez (2), C. Mata (2), JV. Medrano (2), A. Montagud (2), C. Navarrete (2), E. Navarro (1), G. Rodrigo (1), M. Baguena (1), P. Tortosa (3), P. Fernandez-de-Cordoba (1), A. Ferrando (2), J. Salgado (2), J. Urchueguia (1), A. Jaramillo (3).

1 Universidad Politecnica de Valencia, Spain

2 Universitat de Valencia, Spain

3 Ecole Polytechnique, France

Usage and Biology

Sequence and Features