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Type IX secretion system PorM and gliding machinery GldM form extended arches spanning the periplasmic space
- Source :
- Nature Communications, Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-017-02784-7⟩, Nature Communications, 2018, 9 (1), ⟨10.1038/s41467-017-02784-7⟩, Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018), 'Nature Communications ', vol: 9, pages: 429-1-429-8 (2018)
- Publication Year :
- 2018
- Publisher :
- HAL CCSD, 2018.
-
Abstract
- 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.<br />No structural data for the bacterial type IX secretion system (T9SS) are available so far. Here, the authors present the crystal structures of the periplasmic domains from two major T9SS components PorM and GldM, which span most of the periplasmic space, and propose a putative model of the T9SS core membrane complex.
- Subjects :
- 0301 basic medicine
crystal structure
bacterial pathogenesis
Operon
Protein Conformation
Science
[SDV]Life Sciences [q-bio]
030106 microbiology
General Physics and Astronomy
Flavobacterium
General Biochemistry, Genetics and Molecular Biology
Article
gliding machinery
03 medical and health sciences
Protein structure
Bacterial Proteins
Escherichia coli
Inner membrane
Animals
[SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biochemistry [q-bio.BM]
lcsh:Science
Porphyromonas gingivalis
Bacterial Secretion Systems
ComputingMilieux_MISCELLANEOUS
Multidisciplinary
biology
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Structural Biology [q-bio.BM]
Chemistry
[SDV.BBM.BM]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular biology
[SDV.BBM.MN]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Molecular Networks [q-bio.MN]
General Chemistry
Periplasmic space
biology.organism_classification
[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology
Cell biology
Transport protein
[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
[SDV.BBM.BS]Life Sciences [q-bio]/Biochemistry, Molecular Biology/Biomolecules [q-bio.BM]
030104 developmental biology
Helix
Periplasm
lcsh:Q
Bacterial outer membrane
Camelids, New World
dental diseases
type IX secretion system
Subjects
Details
- Language :
- English
- ISSN :
- 20411723
- Database :
- OpenAIRE
- Journal :
- Nature Communications, Nature Communications, Nature Publishing Group, 2018, 9 (1), ⟨10.1038/s41467-017-02784-7⟩, Nature Communications, 2018, 9 (1), ⟨10.1038/s41467-017-02784-7⟩, Nature Communications, Vol 9, Iss 1, Pp 1-8 (2018), 'Nature Communications ', vol: 9, pages: 429-1-429-8 (2018)
- Accession number :
- edsair.doi.dedup.....529f87a3b00ba61857b1c5a12b5bdf7a