Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 Å

John K. Lee, David Kozono, Jonathan Remis, Yoshichika Kitagawa, Peter Agre, Robert M. Stroud

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140 Scopus citations


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-Å 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.

Original languageEnglish (US)
Pages (from-to)18932-18937
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number52
StatePublished - Dec 27 2005


  • Gas
  • Integral membrane protein
  • Water channel
  • X-ray crystallography


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