Difference between revisions of "Part:BBa K525403"

Revision as of 18:13, 21 September 2011

S-Layer SbpA from Lysinibacillus sphaericus with T7/lac

S-Layer SbpA from Lysinbacillus sphaericus

S-layers (crystalline bacterial surface layer) are crystal-like layers consisting of multiple protein monomers and can be found in various (archae-)bacteria. They constitute the outermost part of the cell wall. Especially their ability for self-assembly into distinct geometries is of scientific interest. At phase boundaries, in solutions and on a variety of surfaces they form different lattice structures. The geometry and arrangement is determined by the C-terminal self assembly-domain, which is specific for each S-layer protein. The most common lattice geometries are oblique, square and hexagonal. By modifying the characteristics of the S-layer through combination with functional groups and protein domains as well as their defined position and orientation to eachother (determined by the S-layer geometry) it is possible to realize various practical applications ([http://onlinelibrary.wiley.com/doi/10.1111/j.1574-6968.2006.00573.x/full Sleytr et al., 2007]).

Usage and Biology

S-layer proteins can be used as scaffold for nanobiotechnological applications and devices by e.g. fusing the S-layer's self-assembly domain to other functional protein domains. It is possible to coat surfaces and liposomes with S-layers. A big advantage of S-layers: after expressing in E. coli and purification, the nanobiotechnological system is cell-free. This enhances the biological security of a device.

This S-layer gene is downsteam of a T7 / lac fusion promoter and in the Freiburg BioBrick Assembly standard so functional protein domains can easily be fused to its N-terminus and expressed and purified afterwards. SbpA was characterized with BBa_K525405.

Important parameters

Sequence and Features