Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 20, Issue 11, Pages 1318-U247Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.2689
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Funding
- Swiss National Science Foundation [PP00P3_128419]
- European Research Council [MOMP 281764]
- Werner-Siemens Foundation
- Swiss National Science Foundation (SNF) [PP00P3_128419] Funding Source: Swiss National Science Foundation (SNF)
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TamA is an Escherichia coli Omp85 protein involved in autotransporter biogenesis. It comprises a 16-stranded transmembrane. beta-barrel and three POTRA domains. The 2.3-angstrom crystal structure reveals that the TamA barrel is closed at the extracellular face by a conserved lid loop. The C-terminal beta-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.
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