P.69 Pertactin Structure and Function: Difference between revisions
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==Introduction== | ==Introduction== | ||
Pertactin is a virulence toxin of ''Bordetella pertussis'' and close relatives, such as ''Bordetella parapertussis''. It is an outer surface membrane protein involved in the binding of ''B. pertussis'' to host cells, which aids the bacteria in infection of host cells with whooping cough. Many of the conserved regions in this protein, such as its passenger and autotransporter domains, contribute directly to the overall virulence and pathogenicity of these organisms. | '''Pertactin''' is a virulence toxin of ''Bordetella pertussis'' and close relatives, such as ''Bordetella parapertussis''. It is an outer surface membrane protein involved in the binding of ''B. pertussis'' to host cells, which aids the bacteria in infection of host cells with whooping cough. Many of the conserved regions in this protein, such as its passenger and autotransporter domains, contribute directly to the overall virulence and pathogenicity of these organisms. | ||
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. | 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. | ||
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==3D image== | ==3D image== | ||
<Structure load='1dab' size='350' frame='true' align='left' caption='3D image of pertactin' scene='Insert optional scene name here' /> | <Structure load='1dab' size='350' frame='true' align='left' caption='3D image of pertactin (PDB code [[1dab]])' scene='Insert optional scene name here' /> | ||
==Structure and Protein Adhesion Properties== | ==Structure and Protein Adhesion Properties== | ||
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One of these features is the <scene name='71/716564/Arg_gly_asp/1'>Arg-Gly-Asp (RGD) tripeptide motif</scene> that allows for protein-protein interactions <ref name="EMS" />. This motif has been found in several proteins, and has been shown to support cell adhesion in most cases. A subset of cell-surface proteins, called integrins, act as receptors for cell adhesion molecules. These integrins recognize the RGD motif within their ligands, and allow for cell-substratum and cell-cell interactions <ref>D'Souza, S. E., Ginsberg, M. H., & Plow, E. F. (1991). Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends In Biochemical Sciences, 16(7), 246-250.</ref>. | One of these features is the <scene name='71/716564/Arg_gly_asp/1'>Arg-Gly-Asp (RGD) tripeptide motif</scene> that allows for protein-protein interactions <ref name="EMS" />. This motif has been found in several proteins, and has been shown to support cell adhesion in most cases. A subset of cell-surface proteins, called integrins, act as receptors for cell adhesion molecules. These integrins recognize the RGD motif within their ligands, and allow for cell-substratum and cell-cell interactions <ref>D'Souza, S. E., Ginsberg, M. H., & Plow, E. F. (1991). Arginyl-glycyl-aspartic acid (RGD): a cell adhesion motif. Trends In Biochemical Sciences, 16(7), 246-250.</ref>. | ||
Additionally, P.69 contains two <scene name='71/716564/Proline/3'>proline-rich regions</scene> which are thought to provide important binding sites, and are characteristic of proteins exhibiting binding capabilities <ref name="EMS" />. Proline is a very unusual amino acid, and its structure limits the possible conformations it can adopt. The rigidity of these structures allow for reliable binding sites in many different proteins especially when chains of proline are bound to each other. These regions are typically non-specific, and allow for rapid binding. This is advantageous due to the wide range of ligands that can be bound, increasing the versatility of the proteins that utilize these regions <ref>Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins. Biochemical Journal, 297(Pt 2), 249–260.</ref>. | Additionally, P.69 contains two <scene name='71/716564/Proline/3'>proline-rich regions</scene> which are thought to provide important binding sites, and are characteristic of proteins exhibiting binding capabilities <ref name="EMS" />. Proline is a very unusual amino acid, and its structure limits the possible conformations that it can adopt. The rigidity of these structures allow for reliable binding sites in many different proteins especially when chains of proline are bound to each other. These regions are typically non-specific, and allow for rapid binding. This is advantageous due to the wide range of ligands that can be bound, increasing the versatility of the proteins that utilize these regions <ref>Williamson, M. P. (1994). The structure and function of proline-rich regions in proteins. Biochemical Journal, 297(Pt 2), 249–260.</ref>. | ||
The linear form of pertactin that protrudes from the surface of ''B. pertussis'' also has a high surface area that could be well suited for targeting mammalian cells <ref name="EMS" />. Studies have shown that adhesive area strongly affects integrin binding and adhesion strength. The positioning of binding regions also affects adhesion strength, making the combination of these two factors particularly important for proteins that serve this function <ref>Gallant, N. D., Michael, K. E., & García, A. J. (2005). Cell Adhesion Strengthening: Contributions of Adhesive Area, Integrin Binding, and Focal Adhesion Assembly. Molecular Biology of the Cell, 16(9), 4329–4340.</ref>. | The linear form of pertactin that protrudes from the surface of ''B. pertussis'' also has a high surface area that could be well suited for targeting mammalian cells <ref name="EMS" />. Studies have shown that adhesive area strongly affects integrin binding and adhesion strength. The positioning of binding regions also affects adhesion strength, making the combination of these two factors particularly important for proteins that serve this function <ref>Gallant, N. D., Michael, K. E., & García, A. J. (2005). Cell Adhesion Strengthening: Contributions of Adhesive Area, Integrin Binding, and Focal Adhesion Assembly. Molecular Biology of the Cell, 16(9), 4329–4340.</ref>. | ||
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[[Image:Prn6.png]] | [[Image:Prn6.png]] | ||
==Pertussis Toxin== | |||
{{:Pertussis_Toxin-ATP_Complex}} | {{:Pertussis_Toxin-ATP_Complex}} | ||
Supplemental Information | ==Supplemental Information== | ||
#REDIRECT [[1dab]] | #REDIRECT [[1dab]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
