| Structural highlights
Function
[TAMA_ECOLI] Part of the translocation and assembly module (TAM) autotransporter assembly complex, which functions in translocation of autotransporters across the outer membrane. Has anion selective channel-forming ability, but the physiological relevance of this activity is unclear.[1]
Publication Abstract from PubMed
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-A 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.
The structural basis of autotransporter translocation by TamA.,Gruss F, Zahringer F, Jakob RP, Burmann BM, Hiller S, Maier T Nat Struct Mol Biol. 2013 Sep 22. doi: 10.1038/nsmb.2689. PMID:24056943[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Selkrig J, Mosbahi K, Webb CT, Belousoff MJ, Perry AJ, Wells TJ, Morris F, Leyton DL, Totsika M, Phan MD, Celik N, Kelly M, Oates C, Hartland EL, Robins-Browne RM, Ramarathinam SH, Purcell AW, Schembri MA, Strugnell RA, Henderson IR, Walker D, Lithgow T. Discovery of an archetypal protein transport system in bacterial outer membranes. Nat Struct Mol Biol. 2012 Apr 1;19(5):506-10, S1. doi: 10.1038/nsmb.2261. PMID:22466966 doi:10.1038/nsmb.2261
- ↑ Gruss F, Zahringer F, Jakob RP, Burmann BM, Hiller S, Maier T. The structural basis of autotransporter translocation by TamA. Nat Struct Mol Biol. 2013 Sep 22. doi: 10.1038/nsmb.2689. PMID:24056943 doi:10.1038/nsmb.2689
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