6TOP

Structure of the PorE C-terminal domain, a protein of T9SS from Porphyromonas gingivalis

Replaces:  6I9O

Summary for 6TOP

• Entry DOI: 10.2210/pdb6top/pdb
• Related: 6I9O
• Descriptor: OmpA family protein, GLCNAC(BETA1-4)-MURNAC(1,6-ANHYDRO)-L-ALA-GAMMA-D-GLU-MESO-A2PM-D-ALA, SODIUM ION, ... (5 entities in total)
• Functional Keywords: peptidoglycan binding protein type ix secretion system porphyromonas gingivalis, protein binding
• Biological source: Porphyromonas gingivalis JCVI SC001; More
• Total number of polymer chains: 4
• Total formula weight: 72532.42

Authors

Trinh, T.N.,Cambillau, C.,Roussel, A.,Leone, P. (deposition date: 2019-12-11, release date: 2020-06-17, Last modification date: 2024-05-15)

Primary citation

Trinh, N.T.T.,Tran, H.Q.,Van Dong, Q.,Cambillau, C.,Roussel, A.,Leone, P.
Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment.
Sci Rep, 10:7384-7384, 2020

PubMed Abstract: Porphyromonas gingivalis, the major human pathogen associated to periodontal diseases, utilizes the Bacteroidetes-specific type IX secretion system (T9SS) to export virulence factors. PorE is a periplasmic multi-domain lipoprotein associated to the outer membrane that was recently identified as essential for T9SS function. Little is known on T9SS at the structural level, and in particular its interaction with peptidoglycan. This prompted us to carry out structural studies on PorE full length as well as on its four isolated domains. Here we report the crystal structure of the C-terminal OmpA_C-like putative peptidoglycan-binding domain at 1.55 Å resolution. An electron density volume was identified in the protein cleft, making it possible to build a naturally-occurring peptidoglycan fragment. This result suggests that PorE interacts with peptidoglycan and that PorE could anchor T9SS to the cell wall.

PubMed: 32355178
DOI: 10.1038/s41598-020-64115-z

Experimental method

X-RAY DIFFRACTION (1.55 Å)