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Pum, D. and Sleytr, U.B. (2014) Reassembly of S-Layer Proteins. Nanotechnology, 25, 312001.
https://doi.org/10.1088/0957-4484/25/31/312001

has been cited by the following article:

  • TITLE: Bioinformatic Survey of S-Layer Proteins in Bifidobacteria

    AUTHORS: Juan Li, Yihao Shen, Yatao Jiang, Le He, Zhongke Sun

    KEYWORDS: Bifidobacteria, S-layer Domain Protein, Phylogeny, Homology Modeling, Domain

    JOURNAL NAME: Computational Molecular Bioscience, Vol.8 No.2, June 7, 2018

    ABSTRACT: Surface layer (S-layer) proteins are one of the most commonly observed cell envelope components in both Archaea and Bacteria. It has versatile functions and holds considerable application potential in biotechnology. Bifidobacteria are representative probiotics conferring health promoting properties. However, there is little study of S-layer in bifidobacteria yet. The distribution and characteristics of S-layer in bifidobacteria are unknown. In this study, search for S-layer protein in the identical protein groups in NCBI yielded 49 hits belonging to bifidobacteria. These proteins were annotated as either “S-layer (domain) protein” or “putative S-layer (y) domain protein” that distributed among 26 species of Bifidobacterium genus. Multiple alignments suggest S-layer proteins are relatively conservative. Phylogenetic analysis of 24 S-layer (domain) protein sequences groups them into three distinct clusters, with the majority species in Cluster-2. S-layer (domain) protein has a universe motif DUF4381, though its function is unknown. Meanwhile, two other motifs CARDB and EphA2_TM involved in cell adhesion and cell signaling respectively, presented in most S-layer (domain) protein in bifidobacteria. All S-layer proteins have a typical N-terminal Sec-dependent signal peptide and a C-terminal trans-membrane region. Homological modeling of representative S-layer proteins from each cluster revealed a few unique structural features. All representative S-layer proteins have a plenty of β-meander motif that exclusively composed by β-barrel structural architectures linked together by hairpin loops.