Subangstrom resolution x-ray structure details aquaporin-water interactions

Urszula Kosinska Eriksson, Gerhard Fischer, Rosmarie Friemann, Giray Enkavi, Emad Tajkhorshid, Richard Neutze

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1346-1349
Number of pages4
JournalScience
Volume340
Issue number6138
DOIs
StatePublished - 2013

ASJC Scopus subject areas

  • General

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    Eriksson, U. K., Fischer, G., Friemann, R., Enkavi, G., Tajkhorshid, E., & Neutze, R. (2013). Subangstrom resolution x-ray structure details aquaporin-water interactions. Science, 340(6138), 1346-1349. https://doi.org/10.1126/science.1234306