The structural basis of autotransporter translocation by TamA
The structural basis of autotransporter translocation by TamA
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DOI：
10.1038/nsmb.2689
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发表时间：
2013-11-01
影响因子：
16.8
通讯作者：
Maier, Timm
中科院分区：
文献类型：
--
作者：
Gruss, Fabian;Zaehringer, Franziska;Maier, Timm
TamA 是一种参与自转运蛋白生物发生的大肠杆菌 Omp85 蛋白。它包含 16 股跨膜。 β-桶和三个 POTRA 结构域。 2.3 埃的晶体结构揭示了 TamA 桶在细胞外表面通过保守的盖环封闭。桶的 C 端 β 链形成不寻常的向内扭结，这削弱了侧桶壁并为底物进入脂质双层创建了一个门。
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.