edoc

The structural basis of autotransporter translocation by TamA

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.

Full text not available from this repository.

Official URL: http://edoc.unibas.ch/dok/A6211853

Downloads: Statistics Overview

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)
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
Bibsysno:Link to catalogue
Publisher:Nature Publ. Group
ISSN:1545-9993
Note:Publication type according to Uni Basel Research Database: Journal article
Related URLs:
Identification Number:
Last Modified:13 Dec 2017 12:29
Deposited On:31 Jan 2014 09:50

Repository Staff Only: item control page