Architecture et Fonction des Macromolécules Biologiques, Aix-Marseille Université, UMR 7257, 163 Avenue de Luminy, Case 932, 13009, Marseille, France.
Architecture et Fonction des Macromolécules Biologiques, Centre National de la Recherche Scientifique, UMR 7257, 163 Avenue de Luminy, Case 932, 13009, Marseille, France.
Nat Commun. 2018 Jan 30;9(1):429. doi: 10.1038/s41467-017-02784-7.
Type IX secretion system (T9SS), exclusively present in the Bacteroidetes phylum, has been studied mainly in Flavobacterium johnsoniae and Porphyromonas gingivalis. Among the 18 genes, essential for T9SS function, a group of four, porK-N (P. gingivalis) or gldK-N (F. johnsoniae) belongs to a co-transcribed operon that expresses the T9SS core membrane complex. The central component of this complex, PorM (or GldM), is anchored in the inner membrane by a trans-membrane helix and interacts through the outer membrane PorK-N complex. There is a complete lack of available atomic structures for any component of T9SS, including the PorKLMN complex. Here we report the crystal structure of the GldM and PorM periplasmic domains. Dimeric GldM and PorM, each contain four domains of ~180-Å length that span most of the periplasmic space. These and previously reported results allow us to propose a model of the T9SS core membrane complex as well as its functional behavior.
IX 型分泌系统（T9SS）仅存在于拟杆菌门中，主要在黄杆菌属和牙龈卟啉单胞菌中进行研究。在 18 个对 T9SS 功能至关重要的基因中，有一组四个，porK-N（牙龈卟啉单胞菌）或 gldK-N（黄杆菌属）属于一个共转录操纵子，表达 T9SS 核心膜复合物。该复合物的中心组件，PorM（或 GldM），通过跨膜螺旋锚定在内膜上，并通过外膜 PorK-N 复合物相互作用。目前还没有任何 T9SS 组件（包括 PorKLMN 复合物）的可用原子结构。在这里，我们报告了 GldM 和 PorM 周质域的晶体结构。二聚体 GldM 和 PorM 每个都包含四个约 180-Å 长度的结构域，跨越了大部分周质空间。这些以及以前的报告结果使我们能够提出 T9SS 核心膜复合物及其功能行为的模型。
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