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  Molecular driving forces defining lipid positions around aquaporin-0.

Aponte-Santamaria, C. A., Briones, R., Schenk, A. D., Walz, T., & de Groot, B. L. (2012). Molecular driving forces defining lipid positions around aquaporin-0. Proceedings of the National Academy of Sciences of the United States of America, 109(25), 9887-9892. doi:10.1073/pnas.1121054109.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000F-A216-2 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0027-CDE3-D
Genre: Journal Article

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 Creators:
Aponte-Santamaria, C. A.1, Author              
Briones, R.1, Author              
Schenk, A. D., Author
Walz, T., Author
de Groot, B. L.1, Author              
Affiliations:
1Research Group of Computational Biomolecular Dynamics, MPI for biophysical chemistry, Max Planck Society, ou_578573              

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Free keywords: Electron crystallography; lipd bilayer; atomistic simulations
 Abstract: Lipid–protein interactions play pivotal roles in biological membranes. Electron crystallographic studies of the lens-specific water channel aquaporin-0 (AQP0) revealed atomistic views of such interactions, by providing high-resolution structures of annular lipids surrounding AQP0. It remained unclear, however, whether these lipid structures are representative of the positions of unconstrained lipids surrounding an individual protein, and what molecular determinants define the lipid positions around AQP0. We addressed these questions by using molecular dynamics simulations and crystallographic refinement, and calculated time-averaged densities of dimyristoyl-phosphatidylcholine lipids around AQP0. Our simulations demonstrate that, although the experimentally determined crystallographic lipid positions are constrained by the crystal packing, they appropriately describe the behavior of unconstrained lipids around an individual AQP0 tetramer, and thus likely represent physiologically relevant lipid positions.While the acyl chains were well localized, the lipid head groups were not. Furthermore, in silico mutations showed that electrostatic inter actions do not play a major role attracting these phospholipids towards AQP0. Instead, the mobility of the protein crucially modulates the lipid localization and explains the difference in lipid density between extracellular and cytoplasmic leaflets. Moreover, our simulations support a general mechanism in which membrane proteins laterally diffuse accompanied by several layers of localized lipids, with the positions of the annular lipids being influenced the most by the protein surface. We conclude that the acyl chains rather than the head groups define the positions of dimyristoylphosphatidylcholine lipids around AQP0. Lipid localization is largely determined by the mobility of the protein surface, whereas hydrogen bonds play an important but secondary role.

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Language(s): eng - English
 Dates: 2012-06-072012
 Publication Status: Published in print
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 Rev. Method: Peer
 Identifiers: DOI: 10.1073/pnas.1121054109
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Title: Proceedings of the National Academy of Sciences of the United States of America
Source Genre: Journal
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Pages: - Volume / Issue: 109 (25) Sequence Number: - Start / End Page: 9887 - 9892 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230