结构生物学sturcture biology explore-84.pdfVIP

509 Structure and function of water channels † ‡ Yoshinori Fujiyoshi* , Kaoru Mitsuoka*, Bert L de Groot , Ansgar § ‡ # § Philippsen , Helmut Grubmüller , Peter Agre and Andreas Engel Aquaporins comprise a family of water-transporting membrane puzzling questions concerning the structural basis of these proteins. All aquaporins are efficient water transporters, while remarkable properties. Sequence analysis, cryo-electron sustaining strict selectivity, even against protons, thereby microscopy (cryo-EM), X-ray crystallography and molecular maintaining the proton gradient across the cell membrane. dynamics (MD) simulations have answered many of Recently solved structures of these membrane channels have these questions. helped us to understand this remarkable property. The structure of the Escherichia coli glycerol facilitator GlpF at The atomic model of AQP1 derived from a 3.8 Å resolution 2.2 Å resolution has enabled the refinement of a low-resolution potential map obtained by electron crystallography gave human aquaporin-1 structure. This latter structure has recently the first insight into water specificity and proton blockage been confirmed by the 2.2 Å structure of bovine aquaporin-1. [3••]. This was the first atomic structure of a human Further insights, particularly with respect to the dynamics of membrane protein to be solved. It revealed