Cholera toxin: Difference between revisions
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== Structure == | == Structure == | ||
[[Image:CTX interaction.PNG|left|270px|thumb| Interaction of chains of Cholera toxin [[1xtc]]]] | [[Image:CTX interaction.PNG|left|270px|thumb| Interaction of 7 chains of Cholera toxin.[[1xtc]v]]] | ||
Cholera toxin(CTX) has two types of subunits: subunit A and subunit B. A subunit contains A1 domain, which includes the enzymatic active site, and A2 domain, which has a α–helix tail. The B subunit contains five chains that form a pentameric ring around the central pore in structure; Subunit A and subunit B are assembled by the α–helix tail of A2 domain, which inserts into the central pore. CTX the main virulence factor of the pathogen Vibrio cholerae and cause the major symptom of infection: extreme diarrhea, vomiting, cramps and even death [1][2][3]. | Cholera toxin(CTX) has two types of subunits: subunit A and subunit B. A subunit contains A1 domain, which includes the enzymatic active site, and A2 domain, which has a α–helix tail. The B subunit contains five chains that form a pentameric ring around the central pore in structure; Subunit A and subunit B are assembled by the α–helix tail of A2 domain, which inserts into the central pore. CTX the main virulence factor of the pathogen Vibrio cholerae and cause the major symptom of infection: extreme diarrhea, vomiting, cramps and even death [1][2][3]. | ||
The enzymatic subunit has a globular domain (CTA1) and a long helical domain (CTA2). Once the CTX binds to the cell surface, it is internalized, and its CTA1 domain binds to ADP-ribosylation factor 6 (Arf6) enabling its catalytic activity. | The enzymatic subunit has a globular domain (CTA1) and a long helical domain (CTA2). Once the CTX binds to the cell surface, it is internalized, and its CTA1 domain binds to ADP-ribosylation factor 6 (Arf6) enabling its catalytic activity. | ||
The images at the lower | The images at the lower right correspond to the crystal structure of cholera toxin ([[1xtc]]). The images at left correspond to the annotated interaction of 7 chains of cholera toxins([[1xtc]]) in Proteopedia see [[Toxins]]. | ||
[[Image:1xtc.png|right|280px|thumb|Crystal Structure of Cholera toxin [[1xtc]]]] | [[Image:1xtc.png|right|280px|thumb|Crystal Structure of Cholera toxin [[1xtc]]]] | ||
== mRNA Structure == | == mRNA Structure == | ||
[[Image:CTX_RNA.png|left|280px|thumb|mRNA fold of CTX [[1xtc]]]] | [[Image:CTX_RNA.png|left|280px|thumb|mRNA fold of CTX [[1xtc]]This model is using the minimum free energy model.The colors represent the propensity of each nucleotide to participate in base pairs and whether a predicted base pair is well predicted. The scale ranges from red (highest probability) to blue-violet (lower probability).]] | ||
RNA folding algorithm uses a method to minimize the free energy of the structure so that the RNA molecule is in the most stable form. | RNA folding algorithm uses a method to minimize the free energy of the structure so that the RNA molecule is in the most stable form. | ||
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== Multiple Sequence Alignment == | == Multiple Sequence Alignment == | ||
[[Image:MSA1.jpg|left| | [[Image:MSA1.jpg|left|280px|thumb|BlastP of CTX A subunit]] | ||
'''Selected Sequences:''' | '''Selected Sequences:''' | ||