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- W2034791639 abstract "S-layer proteins are an issue of arising interest due to their ability to form periodical self-assembly nanopore structures. In this work we analyze the self-assembly potential of the recently characterized SslA S-layer protein of Sporosarcina ureae and of truncated SslA derivatives. The SslA protein with an estimated molecular weight of 116 kDa is shown to self-assemble in vitro into the periodic lattices with parameters identical to those of native S-layers formed on the surface of bacterial cells. Recombinant SslA proteins with truncation of N-, C-, or both N- and C-terminal parts were successfully overexpressed in E. coli and showed an aggregation behavior in vitro. A HisXXXHis motif in the central protein part is likely to contribute to self-assembly through the coordination of adjacent SslA monomers by binding the procurable divalent metal ions. (© 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)" @default.
- W2034791639 created "2016-06-24" @default.
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- W2034791639 date "2007-06-01" @default.
- W2034791639 modified "2023-09-25" @default.
- W2034791639 title "Formation of self-assembly nanotemplatesin vitroby native SslA protein and its truncation analysis" @default.
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- W2034791639 doi "https://doi.org/10.1002/pssa.200675354" @default.
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