The research group of Sebastian Hiller, Professor of Structural Biology at the Biozentrum, University of Basel, has now shown for the first time at atomic resolution, that these pore proteins are transported in an unstructured, constantly changing state to the outer bacterial membrane. This landmark study was recently published in the scientific journal “Nature Structural and Molecular Biology”.
The cell membrane of a bacterium is a natural barrier to the environment and at the same time, their door to the world. Gram-negative bacteria surround themselves with two membrane layers. They communicate with the environment through proteins that form tiny pores in the outer cell membrane. How these membrane proteins reach their target destination in the bacterium Escherichia coli could now be observed for the first time at the atomic level by Professor Sebastian Hiller, from the Biozentrum at the University of Basel.Molecular “ferry” ensures safe protein transport
The current study by Hiller provides an exceptional and deep insight into this transport mechanism. The membrane protein is loosely embedded in the solid structure of Skp during transport and does not adopt on a defined spatial structure itself. “Amazingly, the unfolded protein changes its state constantly – faster than thousand times per second and more than ten million times during the crossing,” explained Hiller. “Only through employing modern nuclear magnetic resonance spectroscopy, it has become possible to detect this dynamic behavior within Skp.” Transporting the membrane protein in such a changing state does not require energy and allows for its rapid release at the destination.Dynamic transport as a general principle
Nature Structural & Molecular Biology, Published online 29 September 2013 | doi: 10.1038/nsmb.2677
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