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Subangstrom resolution x-ray structure details aquaporin-water interactions

Tutkimustuotosvertaisarvioitu

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Subangstrom resolution x-ray structure details aquaporin-water interactions. / Eriksson, Urszula Kosinska; Fischer, Gerhard; Friemann, Rosmarie; Enkavi, Giray; Tajkhorshid, Emad; Neutze, Richard.

julkaisussa: Science, Vuosikerta 340, Nro 6138, 2013, s. 1346-1349.

Tutkimustuotosvertaisarvioitu

Harvard

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

APA

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

Vancouver

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

Author

Eriksson, Urszula Kosinska ; Fischer, Gerhard ; Friemann, Rosmarie ; Enkavi, Giray ; Tajkhorshid, Emad ; Neutze, Richard. / Subangstrom resolution x-ray structure details aquaporin-water interactions. Julkaisussa: Science. 2013 ; Vuosikerta 340, Nro 6138. Sivut 1346-1349.

Bibtex - Lataa

@article{2a35c902bdf846f9a74d619ecd009ae3,
title = "Subangstrom resolution x-ray structure details aquaporin-water interactions",
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.",
author = "Eriksson, {Urszula Kosinska} and Gerhard Fischer and Rosmarie Friemann and Giray Enkavi and Emad Tajkhorshid and Richard Neutze",
year = "2013",
doi = "10.1126/science.1234306",
language = "English",
volume = "340",
pages = "1346--1349",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "6138",

}

RIS (suitable for import to EndNote) - Lataa

TY - JOUR

T1 - Subangstrom resolution x-ray structure details aquaporin-water interactions

AU - Eriksson, Urszula Kosinska

AU - Fischer, Gerhard

AU - Friemann, Rosmarie

AU - Enkavi, Giray

AU - Tajkhorshid, Emad

AU - Neutze, Richard

PY - 2013

Y1 - 2013

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=84878943513&partnerID=8YFLogxK

U2 - 10.1126/science.1234306

DO - 10.1126/science.1234306

M3 - Article

VL - 340

SP - 1346

EP - 1349

JO - Science

JF - Science

SN - 0036-8075

IS - 6138

ER -