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  Structure of the hexagonal surface layer on Caulobacter crescentus cells

Bharat, T. A. M., Kureisaite-Ciziene, D., Hardy, G. G., Yu, E. W., Devant, J. M., Hagen, W. J. H., et al. (2017). Structure of the hexagonal surface layer on Caulobacter crescentus cells. Nature Microbiology, 2(7): 17059. doi:10.1038/nmicrobiol.2017.59.

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 Creators:
Bharat, T. A. M., Author
Kureisaite-Ciziene, D., Author
Hardy, G. G., Author
Yu, E. W., Author
Devant, J. M., Author
Hagen, W. J. H., Author
Brun, Y. V., Author
Briggs, John A. G.1, 2, Author           
Lowe, J., Author
Affiliations:
1MRC Laboratory of Molecular Biology, External Organizations, ou_3346673              
2European Molecular Biology Laboratory, External Organizations, Heidelberg, DE, ou_3346677              

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Free keywords: s-layer macromolecular structures model reconstruction visualization refinement software proteins envelope domains Microbiology
 Abstract: Many prokaryotic cells are encapsulated by a surface layer (S-layer) consisting of repeating units of S-layer proteins. S-layer proteins are a diverse class of molecules found in Gram-positive and Gram-negative bacteria and most archaea(1-5). S-layers protect cells from the outside, provide mechanical stability and also play roles in pathogenicity. In situ structural information about this highly abundant class of proteins is scarce, so atomic details of how S-layers are arranged on the surface of cells have remained elusive. Here, using purified Caulobacter crescentus' sole S-layer protein RsaA, we obtained a 2.7 angstrom X-ray structure that shows the hexameric S-layer lattice. We also solved a 7.4 angstrom structure of the S-layer through electron cryotomography and sub-tomogram averaging of cell stalks. The X-ray structure was docked unambiguously into the electron cryotomography map, resulting in a pseudo-atomic-level description of the in vivo S-layer, which agrees completely with the atomic X-ray lattice model. The cellular S-layer atomic structure shows that the S-layer is porous, with a largest gap dimension of 27 angstrom, and is stabilized by multiple Ca2+ ions bound near the interfaces. This study spans different spatial scales from atoms to cells by combining X-ray crystallography with electron cryotomography and sub-nanometre-resolution sub-tomogram averaging.

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Language(s): eng - English
 Dates: 2017
 Publication Status: Published in print
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: WOS:000406925300002
DOI: 10.1038/nmicrobiol.2017.59
ISSN: 2058-5276
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Title: Nature Microbiology
  Alternative Title : Nat. Microbiol
Source Genre: Journal
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Publ. Info: -
Pages: - Volume / Issue: 2 (7) Sequence Number: 17059 Start / End Page: - Identifier: -