de Groot, B. L. and Engel, A. and Grubmüller, H.. (2003) The structure of the aquaporin-1 water channel : a comparison between cryo-electron microscopy and X-ray crystallography. Journal of molecular biology, Vol. 325, H. 3. pp. 485-493.
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Official URL: http://edoc.unibas.ch/dok/A5262393
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Abstract
Three different medium-resolution structures of the human water channel aquaporin-1 (AQP1) have been solved by cryo-electron microscopy (cryo-EM) during the last two years. Recently, the structure of the strongly related bovine AQP1 was solved by X-ray crystallography at higher resolution, allowing a validation of the original medium-resolution structures, and providing a good indication for the strengths and limitations of state of the art cryo-EM methods. We present a detailed comparison between the different models, which shows that overall, the structures are highly similar, deviating less than 2.5 A from each other in the helical backbone regions. The two original cryo-EM structures, however, also show a number of significant deviations from the X-ray structure, both in the backbone positions of the transmembrane helices and in the location of the amino acid side-chains facing the pore. In contrast, the third cryo-EM structure that included information from the X-ray structure of the homologous bacterial glycerol facilitator GlpF and that was subsequently refined against cryo-EM AQP1 data, shows a root mean square deviation of 0.9A from the X-ray structure in the helical backbone regions.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Structural Biology (Engel) |
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UniBasel Contributors: | Engel, Andreas H |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Elsevier |
ISSN: | 0022-2836 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
Last Modified: | 22 Mar 2012 14:21 |
Deposited On: | 22 Mar 2012 13:23 |
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