Crystallization of domains involved in self-assembly of the S-layer protein SbsC

Đordić, Anđela; Egelseer, Eva M.; Tesarz, Manfred; Sleytr, Uwe B.; Keller, Walter; Pavkov‐Keller, Tea

doi:10.1107/s1744309112042650

Cited by 7 publications

(3 citation statements)

References 30 publications

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“…Although enormous efforts were made to elucidate the atomic structure of S-layer proteins by X-ray crystallography, it turned out that originally only truncated forms were accessible, as only these formed three-dimensional crystals [72][73][74]. The first full-length structure of an S-layer protein, namely the S-layer protein SbsB of Geobacillus stearothermophilus PV72/p2 [21], was obtained in 2012 by making use of the nanobody-aided crystallization approach [47].…”

Section: 11 X For Peer Review 8 Of 18mentioning

confidence: 99%

Patterns in Nature—S-Layer Lattices of Bacterial and Archaeal Cells

2021

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Bacterial surface layers (S-layers) have been observed as the outermost cell envelope component in a wide range of bacteria and most archaea. S-layers are monomolecular lattices composed of a single protein or glycoprotein species and have either oblique, square or hexagonal lattice symmetry with unit cell dimensions ranging from 3 to 30 nm. They are generally 5 to 10 nm thick (up to 70 nm in archaea) and represent highly porous protein lattices (30–70% porosity) with pores of uniform size and morphology in the range of 2 to 8 nm. Since S-layers can be considered as one of the simplest protein lattices found in nature and the constituent units are probably the most abundantly expressed proteins on earth, it seems justified to briefly review the different S-layer lattice types, the need for lattice imperfections and the discussion of S-layers from the perspective of an isoporous protein network in the ultrafiltration region. Finally, basic research on S-layers laid the foundation for applications in biotechnology, synthetic biology, and biomimetics.

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Section: 11 X For Peer Review 8 Of 18mentioning

confidence: 99%

Patterns in Nature—S-Layer Lattices of Bacterial and Archaeal Cells

2021

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“…6 However, the details of the interactions between liposomes and Slp remain unclear. In recent years, a series of electron microscopy technologies, such as the thinsectioned, freeze-dried, and freeze-etched methods, 30,[71][72][73][74][75][76][77][78] have been adopted to elucidate the location and ultrastructure of Slp lattices. In addition, information on lattice constants, such as average size, was provided by atomic force microscopy 31,[79][80][81][82][83] and small-angle X-ray scattering.…”

Section: Interactions Between Slp and Liposomesmentioning

confidence: 99%

<p>Slp-coated liposomes for drug delivery and biomedical applications: potential and challenges</p>

Luo¹,

Yang²,

Yao³

et al. 2019

IJN

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Slp forms a crystalline array of proteins on the outermost envelope of bacteria and archaea with a molecular weight of 40-200 kDa. Slp can self-assemble on the surface of liposomes in a proper environment via electrostatic interactions, which could be employed to functionalize liposomes by forming Slp-coated liposomes for various applications. Among the molecular characteristics, the stability, adhesion, and immobilization of biomacromolecules are regarded as the most meaningful. Compared to plain liposomes, Slp-coated liposomes show excellent physicochemical and biological stabilities. Recently, Slp-coated liposomes were shown to specifically adhere to the gastrointestinal tract, which was attributed to the "ligand-receptor interaction" effect. Furthermore, Slp as a "bridge" can immobilize functional biomacromolecules on the surface of liposomes via protein fusion technology or intermolecular forces, endowing liposomes with beneficial functions. In view of these favorable features, Slp-coated liposomes are highly likely to be an ideal platform for drug delivery and biomedical uses. This review aims to provide a general framework for the structure and characteristics of Slp and the interactions between Slp and liposomes, to highlight the unique properties and drug delivery as well as the biomedical applications of the Slp-coated liposomes, and to discuss the ongoing challenges and perspectives.

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“…89 Native and heavy-atom derivative data confirmed the results of the secondary-structure prediction, which indicated that the N-terminal region comprising the first 257 amino acids is mainly organized as α-helices, whereas the middle and C-terminal parts of SbsC consist of loops and β-sheets. 90,91 The crystal-structure model of truncated rSbsC revealed a novel fold, consisting of six separate domains, which are connected by short flexible linkers. Instead of a dissection approach, Baranova et al used a nanobody-aided crystallization system and provided the first 3-D crystal structure of the nontruncated S-layer protein SbsB from Lysinibacillus sphaericus (formerly Bacillus sphaericus ) CCM 2177 with a resolution of 2.4Å.…”

Section: Introductionmentioning

confidence: 99%