6top

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

spinqualitylabelsall models 6top, resolution 1.55Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6top is a 4 chain structure with sequence from Porphyromonas gingivalis JCVI SC001. This structure supersedes the now removed PDB entry 6i9o. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MLD, NA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function T2NEY1_PORGN Publication Abstract from PubMed 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 A 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. Crystal structure of Type IX secretion system PorE C-terminal domain from Porphyromonas gingivalis in complex with a peptidoglycan fragment.,Trinh NTT, Tran HQ, Van Dong Q, Cambillau C, Roussel A, Leone P Sci Rep. 2020 Apr 30;10(1):7384. doi: 10.1038/s41598-020-64115-z. PMID:32355178 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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