Journal
NATURE COMMUNICATIONS
Volume 9, Issue -, Pages -Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-017-02784-7
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Funding
- Centre National de la Recherche Scientifique
- Aix-Marseille Universite
- Agence Nationale de la Recherche [ANR-15-CE11-0019-01]
- French Infrastructure for Integrated Structural Biology (FRISBI)
- Ministere Francais de l'Enseignement
- Agence Nationale de la Recherche (ANR) [ANR-15-CE11-0019] Funding Source: Agence Nationale de la Recherche (ANR)
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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 similar to 180-angstrom 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.
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