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Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A
John K Lee1, David Kozono, Jonathan Remis
1Macromolecular Structure Group, Department of Biochemistry and Biophysics, University of California, S-412C Genentech Hall, 600 16th Street, San Francisco, CA 94143-2240, USA.
Abstract:
To explore the structural basis of the unique selectivity spectrum and conductance of the transmembrane channel protein AqpM from the archaeon Methanothermobacter marburgensis, we determined the structure of AqpM to 1.68-A resolution by x-ray crystallography. The structure establishes AqpM as being in a unique subdivision between the two major subdivisions of aquaporins, the water-selective aquaporins, and the water-plus-glycerol-conducting aquaglyceroporins. In AqpM, isoleucine replaces a key histidine residue found in the lumen of water channels, which becomes a glycine residue in aquaglyceroporins. As a result of this and other side-chain substituents in the walls of the channel, the channel is intermediate in size and exhibits differentially tuned electrostatics when compared with the other subfamilies.
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