Cholera toxin

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 8: Line 8:
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 is the main virulence factor of the pathogen ''Vibrio cholerae'' and cause the major symptom of infection: extreme diarrhea, vomiting, cramps and even death <ref>Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology (4th ed.). McGraw Hill. p. 375. ISBN 0838585299.</ref>,<ref>Faruque SM; Nair GB (editors). (2008). Vibrio cholerae: Genomics and Molecular Biology. Caister Academic Press. ISBN 978-1-904455-33-2.</ref>,<ref>Jennifer McDowall, Cholera Toxin, EMBL-EMI, Interpro</ref>.
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 is the main virulence factor of the pathogen ''Vibrio cholerae'' and cause the major symptom of infection: extreme diarrhea, vomiting, cramps and even death <ref>Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology (4th ed.). McGraw Hill. p. 375. ISBN 0838585299.</ref>,<ref>Faruque SM; Nair GB (editors). (2008). Vibrio cholerae: Genomics and Molecular Biology. Caister Academic Press. ISBN 978-1-904455-33-2.</ref>,<ref>Jennifer McDowall, Cholera Toxin, EMBL-EMI, Interpro</ref>.
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)[http://en.wikipedia.org/wiki/ADP_ribosylation_factor], 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)[http://en.wikipedia.org/wiki/ADP_ribosylation_factor], enabling its catalytic activity.
-
 
+
[[Image:1xtc.png|left|280px|thumb|Crystal Structure of Cholera toxin [[1xtc]]]]
-
 
+
{{Clear}}
-
 
+
-
[[Image:1xtc.png|right|280px|thumb|Crystal Structure of Cholera toxin [[1xtc]]]]
+
-
 
+
== mRNA Structure ==
== mRNA Structure ==
[[Image:CTX_RNA.png|left|280px|thumb|mRNA structure of CTX. The structure is predicted by the method of minimum free energy, using RNAfold WebServer.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).]]
[[Image:CTX_RNA.png|left|280px|thumb|mRNA structure of CTX. The structure is predicted by the method of minimum free energy, using RNAfold WebServer.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).]]

Revision as of 12:58, 18 January 2016

Cholera toxin composed of A1 (grey), A2 (pink) subunit and a pentamer of B subunits (rust, cyan, gold, yellow, purple). 1xtc

Drag the structure with the mouse to rotate

Contents

3D Structures of Cholera toxin

Updated on 18-January-2016

Structure Notation of the RNA of CTX A, CLC RNA Workbench
Structure Notation of the RNA of CTX A, CLC RNA Workbench
Phylogenetic Tree of MSA of CTX, Statistic Method:Maximum Likelihood, made by MEGA 5.05
Phylogenetic Tree of MSA of CTX, Statistic Method:Maximum Likelihood, made by MEGA 5.05

See also Toxins

Multiple Sequence Alignment

Multiple Sequence Alignment-TEXSHADE result.BlastP of CTX A subunit that contains six different species. This is made by Biology Workbench
Multiple Sequence Alignment-TEXSHADE result.BlastP of CTX A subunit that contains six different species. This is made by Biology Workbench

Selected Sequences:

1. Cholera toxin Subunit A

2. Escherichia coli E24377A plasmid pETEC_80, complete sequence

3. Escherichia coli strain 214-III elt operon, complete sequence

4. Vibrio cholerae strain JS9803 prophage Vibrio phage CTX Zot (zot)

5. Vibrio cholera O395 chromosome II, complete sequence

6. Vibrio cholera O1 str. 2010EL-1786 chromosome 1, complete


Reference

  1. ↑ Ryan KJ; Ray CG (editors) (2004). Sherris Medical Microbiology (4th ed.). McGraw Hill. p. 375. ISBN 0838585299.
  2. ↑ Faruque SM; Nair GB (editors). (2008). Vibrio cholerae: Genomics and Molecular Biology. Caister Academic Press. ISBN 978-1-904455-33-2.
  3. ↑ Jennifer McDowall, Cholera Toxin, EMBL-EMI, Interpro
  4. ↑ Jennifer McDowall, Cholera Toxin, EMBL-EMI, Interpro
  5. ↑ Davis B, Waldor M (2003). "Filamentous phages linked to virulence of Vibrio cholerae". Curr Opin Microbiol 6 (1): 35–42. doi:10.1016/S1369-5274(02)00005-X. PMID 12615217.
  6. ↑ Luppi P.H.. "The Discovery of Cholera-Toxin as a Powerful Neuroanatomical Tool". Retrieved 2011-03-23.
  7. ↑ Luppi P.H., Fort P., Jouvet M. Iontophoretic application of unconjugated cholera toxin B subunit (CTb) combined with immunohistochemistry of neurochemical substances: a method for transmitter identification of retrogradely labeled neurons. Brain Res. 534 (1-2) pages : 209-224 (1990)

External Links

PDB ID: 1XTC [1]

MMDB ID: 52036 [2]

PubMed[3]

Proteopedia Page Contributors and Editors (what is this?)

Yang Yang, Michal Harel, Alexander Berchansky

Retrieved from "http://52.214.119.220/wiki/index.php/Cholera_toxin"
Personal tools