We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

6t72

From Proteopedia

Jump to: navigation, search

Structure of the RsaA N-terminal domain bound to LPS

6t72, resolution 3.70Å

Structural highlights

6t72 is a 1 chain structure with sequence from Caulobacter vibrioides CB15. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.7Å
Ligands:
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

SLAP_CAUVC The S-layer is a paracrystalline mono-layered assembly of proteins which coats the surface of bacteria. Probably acts as a physical barrier to parasites and lytic enzymes.

Publication Abstract from PubMed

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.

In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer.,von Kugelgen A, Tang H, Hardy GG, Kureisaite-Ciziene D, Brun YV, Stansfeld PJ, Robinson CV, Bharat TAM Cell. 2020 Jan 23;180(2):348-358.e15. doi: 10.1016/j.cell.2019.12.006. Epub 2019 , Dec 26. PMID:31883796^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ von Kugelgen A, Tang H, Hardy GG, Kureisaite-Ciziene D, Brun YV, Stansfeld PJ, Robinson CV, Bharat TAM. In Situ Structure of an Intact Lipopolysaccharide-Bound Bacterial Surface Layer. Cell. 2020 Jan 23;180(2):348-358.e15. doi: 10.1016/j.cell.2019.12.006. Epub 2019 , Dec 26. PMID:31883796 doi:http://dx.doi.org/10.1016/j.cell.2019.12.006