1S5C | Transerase,Toxin | date | Jan 20, 2004 ![]() |
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title | Cholera Holotoxin With An A-Subunit Y30s Mutation, Crystal Form 1 | ||||||||||||||
authors | C.J.O'Neal, E.I.Amaya, M.G.Jobling, R.K.Holmes, W.G.Hol | ||||||||||||||
compound | source | ||||||||||||||
Molecule: Cholera Enterotoxin, A Chain Chain: A Synonym: Nad(+)--Diphthamide Adp- Ribosyltransferase, Cholera Enterotoxin A Subunit; Ec: 2.4.2.36 Engineered: Yes Mutation: Yes |
Organism_scientific: Vibrio Cholerae Organism_common: Bacteria Gene: Ctxa, Toxa, Vc1457 Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_strain: Bl21(De3) Expression_system_vector_type: Plasmid Expression_system_plasmid: Peia154 | ||||||||||||||
Molecule: Cholera Enterotoxin B-Subunit Chain: D, E, F, G, H Engineered: Yes |
Organism_scientific: Vibrio Cholerae Organism_common: Bacteria Gene: Ctxb, Toxb, Vc1456 Expression_system: Escherichia Coli Expression_system_common: Bacteria Expression_system_strain: Bl21(De3) Expression_system_vector_type: Plasmid Expression_system_plasmid: Peia154 | ||||||||||||||
symmetry | Space Group: P 1 21 1 | R_factor | 0.195 | ||||||||||||
crystal cell |
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method | X-Ray Diffraction | resolution | 2.50 Å | ||||||||||||
ligand | NA | enzyme | NAD+-diphthamide ADP-ribosyltransferase;. ADP-ribosyltransferase;. Mono(ADPribosyl)transferase;. NAD-diphthamide ADP-ribosyltransferase. Transferase E.C.2.4.2.36 BRENDA | ||||||||||||
domain | The four c-terminal residues of the a2 chain occupy the central pore of the holotoxin. Deletion of this residues weakens the interaction between the a subunit and the b pentamer whithout impairing the pentamer formation. | ||||||||||||||
similarity | Belongs to the Enterotoxin_b family. | ||||||||||||||
subunit | The a subunit contains two chains, a1 and a2, linked by a disulfide bridge. The holotoxin (choleragen) consists of a pentameric ring of b subunits whose central pore is occupied by the a subunit. | ||||||||||||||
catalytic activ. | Nad(+) + peptide diphthamide = nicotinamide + peptide n-(adp-d-ribosyl)diphthamide. | ||||||||||||||
genes | HEGFL, HBEGF (H. sapiens); ctxA, ctxB (V. cholerae); EFT2 (S. cerevisiae) | ||||||||||||||
function | This leads to an overproduction of camp and eventually to a hypersecretion of chloride and bicarbonate followed by water, resulting in the characteristic cholera stool. The a2 chain tethers a1 to the pentameric ring. The a1 chain catalyzes the adp-ribosylation of gs alpha, a gtp-binding regulatory protein, to activate the adenylate cyclase. It can bind five gm1 gangliosides. The b subunit pentameric ring directs the a subunit to its target by binding to the gm1 gangliosides present on the surface of the intestinal epithelial cells. It has no toxic activity by itself. | ||||||||||||||
Gene Ontology |
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disease | Diphtheria,susceptibility to | ||||||||||||||
Primary reference | Crystal Structures of an Intrinsically Active Cholera Toxin Mutant Yield Insight into the Toxin Activation Mechanism(,)., O'Neal CJ, Amaya EI, Jobling MG, Holmes RK, Hol WG, Biochemistry 2004 Apr 6;43(13):3772-3782. PMID:15049684 |
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Structure-derived information |
- Domain d1s5ca_, region A [Jmol] [rasmolscript] [script source] - Domain d1s5cd_, region D [Jmol] [rasmolscript] [script source] - Domain d1s5ce_, region E [Jmol] [rasmolscript] [script source] - Domain d1s5cf_, region F [Jmol] [rasmolscript] [script source] - Domain d1s5cg_, region G [Jmol] [rasmolscript] [script source] - Domain d1s5ch_, region H [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
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