6Q0X

The cryo-EM structure of the SNX-BAR Mvp1 tetramer

Summary for 6Q0X

• Entry DOI: 10.2210/pdb6q0x/pdb
• EMDB information: 20555
• Descriptor: Sorting nexin MVP1 (1 entity in total)
• Functional Keywords: mvp1, sorting nexin, snx, px, bar, snx-bar, lipid binding protein
• Biological source: Saccharomyces cerevisiae W303 (Baker's yeast)
• Total number of polymer chains: 4
• Total formula weight: 247611.41

Authors

Sun, D.,Ford, M.G.J.,Zhang, P. (deposition date: 2019-08-02, release date: 2020-04-01, Last modification date: 2024-03-20)

Primary citation

Sun, D.,Varlakhanova, N.V.,Tornabene, B.A.,Ramachandran, R.,Zhang, P.,Ford, M.G.J.
The cryo-EM structure of the SNX-BAR Mvp1 tetramer.
Nat Commun, 11:1506-1506, 2020

PubMed Abstract: Sorting nexins (SNX) are a family of PX domain-containing proteins with pivotal roles in trafficking and signaling. SNX-BARs, which also have a curvature-generating Bin/Amphiphysin/Rvs (BAR) domain, have membrane-remodeling functions, particularly at the endosome. The minimal PX-BAR module is a dimer mediated by BAR-BAR interactions. Many SNX-BAR proteins, however, additionally have low-complexity N-terminal regions of unknown function. Here, we present the cryo-EM structure of the full-length SNX-BAR Mvp1, which is an autoinhibited tetramer. The tetramer is a dimer of dimers, wherein the membrane-interacting BAR surfaces are sequestered and the PX lipid-binding sites are occluded. The N-terminal low-complexity region of Mvp1 is essential for tetramerization. Mvp1 lacking its N-terminus is dimeric and exhibits enhanced membrane association. Membrane binding and remodeling by Mvp1 therefore requires unmasking of the PX and BAR domain lipid-interacting surfaces. This work reveals a tetrameric configuration of a SNX-BAR protein that provides critical insight into SNX-BAR function and regulation.

PubMed: 32198400
DOI: 10.1038/s41467-020-15110-5

Experimental method

ELECTRON MICROSCOPY (4.2 Å)