9RHR

FusA (ferredoxin receptor from Pectobacterium atrosepticum) in the presence of Ra-LPS

This is a non-PDB format compatible entry.

Summary for 9RHR

• Entry DOI: 10.2210/pdb9rhr/pdb
• EMDB information: 53974
• Descriptor: Ferredoxin receptor (1 entity in total)
• Functional Keywords: outer membrane protein, transmembrane beta-barrel, tonb-dependent transporter, membrane protein
• Biological source: Pectobacterium atrosepticum SCRI1043
• Total number of polymer chains: 1
• Total formula weight: 97786.56

Authors

Machin, J.M.,Ranson, N.A. (deposition date: 2025-06-10, release date: 2025-12-03, Last modification date: 2025-12-24)

Primary citation

Machin, J.M.,Mosbahi, K.,Prakaash, D.,Radford, S.E.,Walker, D.,Kalli, A.C.,Ranson, N.A.
The structure of the bacterial outer membrane transporter FusA enabled by addition of the native lipid lipopolysaccharide.
J Struct Biol X, 12:100141-100141, 2025

PubMed Abstract: Lipopolysaccharide (LPS) is a glycolipid found uniquely in the outer membrane of diderm bacteria, formed of 4-7 acyl chains covalently linked to an extended polysaccharide chain. While a few examples of the interaction between LPS and outer membrane proteins (OMPs) have been structurally characterised, either experimentally or computationally, the precise nature of LPS-OMP interactions and their functional consequences remains unclear. Here, we show that the addition of LPS facilitated cryoEM structure determination of FusA, a 100 kDa TonB-dependent outer membrane transporter from . A 2.8 Å structure combined with molecular dynamics of FusA with different LPS models reveals LPS binding sites with a strong LPS interaction site located adjacent to the β-seam region of the FusA β-barrel. The requirement of lipid binding for successful structure determination indicates a stabilisation of the protein, which in turn suggests a potential method for solving other, small OMPs and membrane proteins. Further, it hints at how LPS may mediate protein conformation and thus how LPS and OMPs can work in concert to maintain a structural and functional OM.

PubMed: 41399487
DOI: 10.1016/j.yjsbx.2025.100141

Experimental method

ELECTRON MICROSCOPY (2.4 Å)