TUTCRIS - Tampereen teknillinen yliopisto

TUTCRIS

Subangstrom resolution x-ray structure details aquaporin-water interactions

Tutkimustuotosvertaisarvioitu

Yksityiskohdat

AlkuperäiskieliEnglanti
Sivut1346-1349
Sivumäärä4
JulkaisuScience
Vuosikerta340
Numero6138
DOI - pysyväislinkit
TilaJulkaistu - 2013
OKM-julkaisutyyppiA1 Alkuperäisartikkeli

Tiivistelmä

Aquaporins are membrane channels that facilitate the flow of water across biological membranes. Two conserved regions are central for selective function: the dual asparagine-proline-alanine (NPA) aquaporin signature motif and the aromatic and arginine selectivity filter (SF). Here, we present the crystal structure of a yeast aquaporin at 0.88 angstrom resolution. We visualize the H-bond donor interactions of the NPA motif's asparagine residues to passing water molecules; observe a polarized water-water H-bond configuration within the channel; assign the tautomeric states of the SF histidine and arginine residues; and observe four SF water positions too closely spaced to be simultaneously occupied. Strongly correlated movements break the connectivity of SF waters to other water molecules within the channel and prevent proton transport via a Grotthuss mechanism.

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