6T72

Structure of the RsaA N-terminal domain bound to LPS

6T72 の概要

• エントリーDOI: 10.2210/pdb6t72/pdb
• EMDBエントリー: 10389
• 分子名称: S-layer protein, 4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-4-acetamido-4,6-dideoxy-alpha-D-mannopyranose-(1-3)-beta-D-mannopyranose, CALCIUM ION (3 entities in total)
• 機能のキーワード: s-layer lps rsaa, structural protein
• 由来する生物種: Caulobacter vibrioides CB15
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28104.71

構造登録者

von Kuegelgen, A.,Bharat, T.A.M. (登録日: 2019-10-21, 公開日: 2020-01-15, 最終更新日: 2024-05-22)

主引用文献

von Kugelgen, A.,Tang, H.,Hardy, G.G.,Kureisaite-Ciziene, D.,Brun, Y.V.,Stansfeld, P.J.,Robinson, C.V.,Bharat, T.A.M.
In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer.
Cell, 180:348-358.e15, 2020

PubMed Abstract: 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.

PubMed: 31883796
DOI: 10.1016/j.cell.2019.12.006

実験手法

ELECTRON MICROSCOPY (3.7 Å)