There are membranes wrapped around all of our cells, and single-celled organisms like bacteria, too. But they do more than just hold everything in – tiny tunnel-like pores control the flow of important chemicals in and out. Usually this delicate balance helps life along. But here is a pore-making protein that can kill. The complement membrane attack complex (MAC) assembles from a group of proteins in our blood, triggered by our immune system to punch holes in nasty pathogens like bacteria – its long strands piercing the cell surface while precious chemicals burst out. Examining the structure of MAC using cryogenic electron microscopy allows scientists to spot a crucial step in how these avenging proteins come together – slotting together a series of identical protein pieces into a ring shape, before it can begin to penetrate the cell. This insight may help the design of drugs to help MAC tackle infections.
Image generated from the RCSB Protein Data Bank (PDB), NGL Viewer – AS Rose et al. (2018) doi:10.1093/bioinformatics/bty419
Text summary about research from ARC Centre of Excellence in Advanced Molecular Imaging, Department of Biochemistry and Molecular Biology, Monash University, Victoria, Australia
Data files contained in the PDB archive are free of all copyright restrictions, with attribution
Research published in Nature Communications, August 2018
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