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Protein structure: Peering into the transit pore
Date:2/7/2014

ures with the help of cryo-electron microscopy at the unprecedented resolution of less than 1 nanometer. "This allowed us to determine the spatial conformations of the individual protein strands that make up the channel and to analyze how the channel behaves during its functional cycle," he explains.

Indeed, the researchers were even able to capture a snapshot of the complex at the moment when a protein leaves the channel to be incorporated into the cell membrane. "It turns out that there actually is a side-door within the channel, which opens to allow the protein to diffuse into the membrane," Beckmann says. Interestingly, as the lateral gate opens and the protein exits the channel into the membrane, the plug moves into the central constriction, blocking access to the outside and preventing diffusion of ions through the now empty channel. Surprisingly, proteins destined to cross the membrane do so without altering the position of the plug very much. Instead, an adjacent strand shifts slightly outward, widening the constriction sufficiently to let the protein through the length of the tunnel.

Beckmann and his team now hope to be able to increase the resolution of their snapshots still further. "Our goal is to achieve a resolution of less than 0.4 nm, in order to discern the interactions in molecular detail and understand the dynamic changes that take place in the structure of the channel," he says. In addition, the scientists want to image other membrane protein complexes such as visual pigments and analyze how a single chain of amino acids can function as a dynamically active membrane receptor.


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Contact: Luise Dirscherl
dirscherl@lmu.de
49-892-180-2706
Ludwig-Maximilians-Universitt Mnchen
Source:Eurekalert

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