Gruss, Fabian and Zähringer, Franziska and Jakob, Roman P. and Burmann, Björn M. and Hiller, Sebastian and Maier, Timm. (2013) The structural basis of autotransporter translocation by TamA. Nature structural & molecular biology, Vol. 20, no. 11. pp. 1318-1320.
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Official URL: http://edoc.unibas.ch/dok/A6211853
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Abstract
TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane β-barrel and three POTRA domains. The 2.3-Å crystal structure reveals that the TamA barrel is closed at the extracellular face by a conserved lid loop. The C-terminal β-strand of the barrel forms an unusual inward kink, which weakens the lateral barrel wall and creates a gate for substrate access to the lipid bilayer.
Faculties and Departments: | 05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Hiller) 05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Maier) |
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UniBasel Contributors: | Maier, Timm and Gruss, Fabian and Zähringer, Franziska Ursula and Jakob, Roman Peter and Burmann, Björn M. and Hiller Odermatt, Sebastian |
Item Type: | Article, refereed |
Article Subtype: | Research Article |
Publisher: | Nature Publ. Group |
ISSN: | 1545-9993 |
Note: | Publication type according to Uni Basel Research Database: Journal article |
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Identification Number: |
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Last Modified: | 13 Dec 2017 12:29 |
Deposited On: | 31 Jan 2014 09:50 |
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