6Z7P

Composite model of the Caulobacter crescentus S-layer bound to the O-antigen of lipopolysaccharide

6Z7P の概要

• エントリーDOI: 10.2210/pdb6z7p/pdb
• 関連するPDBエントリー: 5N97 6T72
• EMDBエントリー: 10388 10389 3604
• 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, CALCIUM ION (3 entities in total)
• 機能のキーワード: rsaa s-layer sub-tomogram averaging caulobacter lipopolysaccharide o-antigen, structural protein
• 由来する生物種: Caulobacter vibrioides (strain ATCC 19089 / CB15)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 100532.01

構造登録者

Bharat, T.A.M.,von Kugelgen, A. (登録日: 2020-06-01, 公開日: 2020-07-15, 最終更新日: 2024-05-15)

主引用文献

von Kuegelgen, 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 (4.8 Å)