Pertactin sandbox1: Difference between revisions

← Older edit Newer edit →

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Kimberly Eldridge, Melissa Gray, Rachel Korba, Claire Gormley, Zackary Zayakosky

@@ Line 2: / Line 2: @@
 Pertactin is a virulence toxin of ''Bordetella parapertussis'' and close relatives, such as ''Bordetella pertussis''. It is an outer surface membrane protein involved in the binding of ''B. parapertussis'' to host cells, which aids the bacteria in infection of host cells with whooping cough.
-Autotransporters make up the largest protein family family in Gram-negative bacteria. They are usually comprised of a C-terminal beta-barrel-shaped transporter domain anchored in the outer membrane and an N-terminal passenger domain that crosses the outer membrane through the beta barrel (Figure 1a). The autotransporter is considered a virulence factor with the passenger domain contributing to the virulence of the pathogen. This N-terminal domain is similar in structure between different species, but the functions vary greatly. However, the C terminal beta-barrel domain is a highly conserved structure for transport across the membrane but can vary greatly in the sequence. Many factors including biogenesis, use of accessory proteins, and fate of the beta-barrel translocator are not well known.
+Autotransporters make up the largest protein family in Gram-negative bacteria. They are usually comprised of a C-terminal beta-barrel-shaped transporter domain anchored in the outer membrane and an N-terminal passenger domain that crosses the outer membrane through the beta barrel (Figure 1a). The autotransporter is considered a virulence factor with the passenger domain contributing to the virulence of the pathogen. This N-terminal domain is similar in structure between different species, but the functions vary greatly. However, the C terminal beta-barrel domain is a highly conserved structure for transport across the membrane but can vary greatly in the sequence. Many factors including biogenesis, use of accessory proteins, and fate of the beta-barrel translocator are not well known.
 Seeing that the structure of the passenger domain is similar between various bacteria, it was found that about 97% of them contain an extended right handed beta-helical structure. Specifically, pertactin has a passenger domain with a 16-turn parallel β-helix with a V-shaped cross-section and a hydrophobic core. Each turn contains approximately 25 residues which make up three beta strands that are linked by loops. It is predicted that the alpha-helical passenger domain traverses the hydrophilic pore of the transporter domain after the transporter domain is inserted into the outer membrane <ref name="BEN">Benz, I., & Schmidt, M. (n.d.). Structures and functions of autotransporter proteins in microbial pathogens. International Journal of Medical Microbiology, 461-468</ref>.