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Updated: Jun 12, 2026

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Method to Visualize and Analyze Membrane Interacting Proteins by Transmission Electron Microscopy

Published on: March 5, 2017

Features critical for membrane binding revealed by DivIVA crystal structure.

Maria A Oliva¹, Sven Halbedel, Stefan M Freund

¹MRC Laboratory of Molecular Biology, Cambridge, UK.

The EMBO Journal

|May 27, 2010

Summary

DivIVA protein structure was elucidated, revealing its essential role in bacterial cell division and chromosome anchoring. Its N-terminal domain binds membranes via hydrophobic and charged residues, crucial for bacterial growth.

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Area of Science:

Microbiology
Structural Biology
Molecular Biology

Background:

DivIVA is a conserved protein in Gram-positive bacteria.
It localizes to cell poles and division sites, sensing membrane curvature.
DivIVA is vital for septum site selection and chromosome anchoring.

Purpose of the Study:

To determine the crystal structure of the DivIVA N-terminal (Nt) domain.
To elucidate the mechanism of DivIVA membrane binding.
To model the full-length DivIVA protein structure.

Main Methods:

X-ray crystallography was used to determine the structures of the Nt and C-terminal (Ct) domains.
Mutagenesis and intragenic suppressor analysis were performed to study membrane binding.
Structural data were used to build a model of full-length DivIVA.

Main Results:

The DivIVA Nt domain forms a parallel coiled-coil capped with loops containing essential hydrophobic and charged residues for membrane binding.
The Ct domain forms a curved tetramer.
A model of the full-length, 30 nm DivIVA protein was constructed.

Conclusions:

DivIVA's structure facilitates its function as a scaffold in bacterial cell division.
Hydrophobic residues likely insert into the membrane, while charged residues interact with the surface.
The structural insights provide a basis for understanding DivIVA's role in bacterial morphogenesis.