Lipid–protein interactions in double-layered two-dimensional AQP0 crystals

Tamir Gonen, Yifan Cheng, Piotr Sliz, Yoko Hiroaki, Yoshinori Fujiyoshi, Stephen C. Harrison and Thomas Walz ()
Additional contact information
Tamir Gonen: Department of Cell Biology
Yifan Cheng: Department of Cell Biology
Piotr Sliz: Harvard Medical School
Yoko Hiroaki: Kyoto University, Oiwake
Yoshinori Fujiyoshi: Kyoto University, Oiwake
Stephen C. Harrison: Harvard Medical School
Thomas Walz: Department of Cell Biology

Nature, 2005, vol. 438, issue 7068, 633-638

Abstract: Abstract Lens-specific aquaporin-0 (AQP0) functions as a specific water pore and forms the thin junctions between fibre cells. Here we describe a 1.9 Å resolution structure of junctional AQP0, determined by electron crystallography of double-layered two-dimensional crystals. Comparison of junctional and non-junctional AQP0 structures shows that junction formation depends on a conformational switch in an extracellular loop, which may result from cleavage of the cytoplasmic amino and carboxy termini. In the centre of the water pathway, the closed pore in junctional AQP0 retains only three water molecules, which are too widely spaced to form hydrogen bonds with each other. Packing interactions between AQP0 tetramers in the crystalline array are mediated by lipid molecules, which assume preferred conformations. We were therefore able to build an atomic model for the lipid bilayer surrounding the AQP0 tetramers, and we describe lipid–protein interactions.

Date: 2005
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature04321 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:438:y:2005:i:7068:d:10.1038_nature04321

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature04321

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().