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-Structure paper
タイトル | In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer. |
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ジャーナル・号・ページ | Cell, Vol. 180, Issue 2, Page 348-358.e15, Year 2020 |
掲載日 | 2020年1月23日 |
![]() | Andriko von Kügelgen / Haiping Tang / Gail G Hardy / Danguole Kureisaite-Ciziene / Yves V Brun / Phillip J Stansfeld / Carol V Robinson / Tanmay A M Bharat / ![]() ![]() ![]() |
PubMed 要旨 | Most bacterial and all archaeal cells are encapsulated by a paracrystalline, protective, and cell-shape-determining proteinaceous surface layer (S-layer). On Gram-negative bacteria, S-layers are ...Most bacterial and all archaeal cells are encapsulated by a paracrystalline, protective, and cell-shape-determining proteinaceous surface layer (S-layer). On Gram-negative bacteria, S-layers are anchored to cells via lipopolysaccharide. Here, we report an electron cryomicroscopy structure of the Caulobacter crescentus S-layer bound to the O-antigen of lipopolysaccharide. Using native mass spectrometry and molecular dynamics simulations, we deduce the length of the O-antigen on cells and show how lipopolysaccharide binding and S-layer assembly is regulated by calcium. Finally, we present a near-atomic resolution in situ structure of the complete S-layer using cellular electron cryotomography, showing S-layer arrangement at the tip of the O-antigen. A complete atomic structure of the S-layer shows the power of cellular tomography for in situ structural biology and sheds light on a very abundant class of self-assembling molecules with important roles in prokaryotic physiology with marked potential for synthetic biology and surface-display applications. |
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手法 | EM (サブトモグラム平均) / EM (単粒子) |
解像度 | 3.7 - 4.8 Å |
構造データ | EMDB-10388: In situ structure of the Caulobacter crescentus S-layer EMDB-10389, PDB-6t72: |
化合物 | ![]() ChemComp-CA: |
由来 |
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![]() | STRUCTURAL PROTEIN / S-layer LPS RsaA / RsaA S-layer sub-tomogram averaging Caulobacter lipopolysaccharide O-antigen |