6Z7P
Composite model of the Caulobacter crescentus S-layer bound to the O-antigen of lipopolysaccharide
Summary for 6Z7P
Entry DOI | 10.2210/pdb6z7p/pdb |
Related | 5N97 6T72 |
EMDB information | 10388 10389 3604 |
Descriptor | 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) |
Functional Keywords | rsaa s-layer sub-tomogram averaging caulobacter lipopolysaccharide o-antigen, structural protein |
Biological source | Caulobacter vibrioides (strain ATCC 19089 / CB15) |
Total number of polymer chains | 1 |
Total formula weight | 100532.01 |
Authors | Bharat, T.A.M.,von Kugelgen, A. (deposition date: 2020-06-01, release date: 2020-07-15, Last modification date: 2024-05-15) |
Primary citation | 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 Cited by 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: 31883796DOI: 10.1016/j.cell.2019.12.006 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (4.8 Å) |
Structure validation
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