SidC is one of the effectors delivered by Legionella pneumophila into the host cell. Like its paralogue SdcA, SidC anchor on the Legionella-containing vacuole (LCV) through binding to phosphatidylinositol-4-phosphate (PI(4)P) to facilitate the recrui ...
SidC is one of the effectors delivered by Legionella pneumophila into the host cell. Like its paralogue SdcA, SidC anchor on the Legionella-containing vacuole (LCV) through binding to phosphatidylinositol-4-phosphate (PI(4)P) to facilitate the recruitment of endoplasmic reticulum (ER) proteins. SidC is organised into four domains that are packed into an arch-like shape: the N- terminal SNL domain (Pfam:PF18219), the INS domain (which is inserted within the SNL domain), the PI(4)P binding domain or P4C domain (this entry), and a C-terminal domain (Pfam:PF20875). The lipid binding domain shows a four alpha-helix bundle with one end sealed by a C-terminal short beta hairpin and a highly positively charged pocket at the other end formed by two loops connecting the alpha-helices.s This pocket is thought to be the binding site, responsible for the stimulation of the E3 ligase activity of the SNL domain [1].
SidC is one of the effectors delivered by Legionella pneumophila into the host cell. Like its paralogue SdcA, SidC anchor on the Legionella-containing vacuole (LCV) to facilitate the recruitment of endoplasmic reticulum (ER) proteins. This protein is ...
SidC is one of the effectors delivered by Legionella pneumophila into the host cell. Like its paralogue SdcA, SidC anchor on the Legionella-containing vacuole (LCV) to facilitate the recruitment of endoplasmic reticulum (ER) proteins. This protein is organised into four domains that are packed into an arch-like shape: the N- terminal SNL domain (Pfam:PF18219), the INS domain (which is inserted within the SNL domain), the P4C domain, and a C-terminal domain. This entry represents the latter, which shows an alpha-helical fold. Its function is unknown [1].
This is the N-terminal domain of SidC present in Legionella pneumophilia. SidC appears to be involved in modulating mammalian trafficking by promoting the communication between ER-derived vesicles and the Legionella containing vacuole. The N-terminal ...
This is the N-terminal domain of SidC present in Legionella pneumophilia. SidC appears to be involved in modulating mammalian trafficking by promoting the communication between ER-derived vesicles and the Legionella containing vacuole. The N-terminal domain (SidC-N) has a novel fold with 4 potential subdomains. SidC-N does not show structural similarity to any known protein domain in the protein data bank [1].
