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Publication Abstract from PubMed
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.
Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A.,Lee JK, Kozono D, Remis J, Kitagawa Y, Agre P, Stroud RM Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18932-7. Epub 2005 Dec 16. PMID:16361443[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑Lee JK, Kozono D, Remis J, Kitagawa Y, Agre P, Stroud RM. Structural basis for conductance by the archaeal aquaporin AqpM at 1.68 A. Proc Natl Acad Sci U S A. 2005 Dec 27;102(52):18932-7. Epub 2005 Dec 16. PMID:16361443
