Abstract：
:Aquaporin-1 (AQP1) is an abundant protein in human erythrocyte membranes which functions as a specific and constitutively active water conducting pore. Solubilized and isolated as tetramer, it forms well-ordered two-dimensional (2D) crystals when reconstituted in the presence of lipids. Several high resolution projection maps of AQP1 have been determined, but information on its three-dimensional (3D) mass distribution is sparse. Here, we present surface reliefs at 0.9 nm resolution that were calculated from freeze-dried unidirectionally metal-shadowed AQP1 crystals as well as surface topographs recorded with the atomic force microscope of native crystals in buffer solution. Our results confirm the 3D map of negatively stained AQP1 crystals, which exhibited tetramers with four major protrusions on one side and a large central cavity on the other side of the membrane. Digestion of AQP1 crystals with carboxypeptidase Y, which cleaves off a 5 kDa intracellular C-terminal fragment, led to a reduction of the major protrusions, suggesting that the central cavity of the tetramer faces the outside of the cell. To interpret the results, sequence based structure predictions served as a guide.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Walz T,Tittmann P,Fuchs KH,Müller DJ,Smith BL,Agre P,Gross H,Engel Adoi
10.1006/jmbi.1996.0686subject
Has Abstractpub_date
1996-12-20 00:00:00pages
907-18issue
5eissn
0022-2836issn
1089-8638pii
S0022-2836(96)90686-5journal_volume
264pub_type
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