8Z5G

Cryo-EM structure of E.coli SPFH-NfeD family protein complex QmcA-YbbJ

This is a non-PDB format compatible entry.

Summary for 8Z5G

• Entry DOI: 10.2210/pdb8z5g/pdb
• EMDB information: 39773
• Descriptor: Protein QmcA, Inner membrane protein YbbJ (2 entities in total)
• Functional Keywords: complex, membrane protein
• Biological source: Escherichia coli (strain K12); More
• Total number of polymer chains: 52
• Total formula weight: 1319104.75

Authors

Qiao, Z.,Gao, Y.G. (deposition date: 2024-04-18, release date: 2024-08-21, Last modification date: 2024-10-23)

Primary citation

Tan, K.A.,Qiao, Z.,Lim, Z.Z.E.,Yeo, J.Y.,Yong, Y.,Do, P.H.,Rya, E.,Gao, Y.G.
Cryo-EM structure of the SPFH-NfeD family protein complex QmcA-YbbJ.
Structure, 32:1603-, 2024

PubMed Abstract: The SPFH (stomatin, prohibitin, flotillin, and HflK/C) protein family is universally present and encompasses the evolutionarily conserved SPFH domain. These proteins are predominantly localized in lipid raft and implicated in various biological processes. The NfeD (nodulation formation efficiency D) protein family is often encoded in tandem with SPFH proteins, suggesting a close functional relationship. Here, we elucidate the cryoelectron microscopy (cryo-EM) structure of the Escherichia coli QmcA-YbbJ complex belonging to the SPFH and NfeD families, respectively. Our findings reveal that the QmcA-YbbJ complex forms an intricate cage-like structure composed of 26 copies of QmcA-YbbJ heterodimers. The transmembrane helices of YbbJ act as adhesive elements bridging adjacent QmcA molecules, while the oligosaccharide-binding domain of YbbJ encapsulates the SPFH domain of QmcA. Our structural study significantly contributes to understanding the functional role of the NfeD protein family and sheds light on the interplay between SPFH and NfeD family proteins.

PubMed: 39181124
DOI: 10.1016/j.str.2024.07.022

Experimental method

ELECTRON MICROSCOPY (2.9 Å)