Difference between revisions of "Part:BBa K525401"
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<partinfo>BBa_K525401 short</partinfo> | <partinfo>BBa_K525401 short</partinfo> | ||
− | S-Layer | + | [[Image:Bielefeld-Germany2011-S-Layer-Geometrien.jpg|300px|thumb|right]] |
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+ | S-layer SbpA from ''Lysinbacillus sphaericus'' | ||
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+ | 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]). | ||
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===Usage and Biology=== | ===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. | ||
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+ | This S-layer gene is in the Freiburg BioBrick Assembly standard so functional protein domains can easily be fused to its C- or N-terminus. SbpA was characterized with <partinfo>K525405</partinfo>. | ||
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Latest revision as of 03:15, 22 September 2011
S-Layer SbpA from Lysinibacillus sphaericus
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 in the Freiburg BioBrick Assembly standard so functional protein domains can easily be fused to its C- or N-terminus. SbpA was characterized with BBa_K525405.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 32
Illegal BglII site found at 149
Illegal XhoI site found at 1924 - 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 4
Illegal AgeI site found at 3121 - 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 421
Illegal BsaI.rc site found at 550