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August 28, 2008

Structural Biology

Camera Iris Mechanism Saves Bacteria

Complementary approaches capture ion channel in its open form

Carmen Drahl

Videos

Two simulations show the camera-iris-like opening mechanism that the bacterial ion channel MscS uses to respond to increased tension on the cell membrane.

View looking into the channel pore

Courtesy of James H. Naismith * Macromedia Flash Player 8 is required to view video.

Side view of the channel

Courtesy of James H. Naismith * Macromedia Flash Player 8 is required to view video.

Bacteria experience massive pressures against their membranes when they're suddenly exposed to fresh water, but they survive because they possess pressure-relieving protein floodgates in the form of ion channels. Now, two independent research teams propose that one such molecular safety valve works like a camera's iris.

Courtesy of James Naismith View Enlarged Image
MscS ion channel widens like a camera???s iris to relieve membrane pressure.

Structural data for the closed form of MscS, a bacterial ion channel that opens in response to increases in membrane tension, already exist. However, trapping MscS in its open form has proven to be a challenge. In one study, led by Eduardo Perozo of the University of Chicago, researchers used cone-shaped lipids to alter the pressure on membrane-embedded MscS and open it (Science 2008, 321, 1210). They characterized the channel with electron paramagnetic resonance spectroscopy.

Meanwhile, James H. Naismith of the University of St. Andrews and Ian R. Booth of the University of Aberdeen, both in Scotland, led a team that crystallized a mutant MscS that is stuck in the open state and determined its X-ray structure (Science 2008, 321, 1179). Both teams suggest that the irislike motion removes a hydrophobic seal from the channel pore, thereby allowing water and ions through.

Two simulations show the camera-iris-like opening mechanism that the bacterial ion channel MscS uses to respond to increased tension on the cell membrane.

View looking into the channel pore

Courtesy of James H. Naismith

Side view of the channel

Courtesy of James H. Naismith

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ISSN 0009-2347
Copyright © 2009 American Chemical Society

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