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59  structures 61  species 2  interactions 100  sequences 5  architectures

Family: Binary_toxB (PF03495)

Summary: Clostridial binary toxin B/anthrax toxin PA

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This is the Wikipedia entry entitled "AB toxin". More...

AB toxin Edit Wikipedia article

ADPrib_exo_Tox
PDB 1giq EBI.jpg
crystal structure of the enzymatic componet of iota-toxin from clostridium perfringens with nadh
Identifiers
Symbol ADPrib_exo_Tox
Pfam PF03496
Pfam clan CL0084
InterPro IPR003540
SCOP 1giq
SUPERFAMILY 1giq
Binary_toxB
PDB 1tzo EBI.jpg
crystal structure of the anthrax toxin protective antigen heptameric prepore
Identifiers
Symbol Binary_toxB
Pfam PF03495
InterPro IPR003896
SCOP 1acc
SUPERFAMILY 1acc
TCDB 1.C.42

The AB toxins are two-component protein complexes secreted by a number of pathogenic bacteria. They can be classified as Type III toxins because they interfere with internal cell function.[1] They are named AB toxins due to their components: the "A" component is usually the "active" portion, and the "B" component is usually the "binding" portion.[1][2] The "A" subunit possesses enzyme activity, and is transferred to the host cell following a conformational change in the membrane-bound transport "B" subunit.[3] Among the toxins produced by certain Clostridium spp. are the binary exotoxins. These proteins consist of two independent polypeptides, which correspond to the A/B subunit moieties. The enzyme component (A) enters the cell through endosomes produced by the oligomeric binding/translocation protein (B), and prevents actin polymerisation through ADP-ribosylation of monomeric G-actin.[3][4][5]

Members of the "A" binary toxin family include C. perfringens iota toxin Ia,[3] C. botulinum C2 toxin CI,[4] and Clostridium difficile ADP-ribosyltransferase .[5] Other homologous proteins have been found in Clostridium spiroforme.[4][5]

Members of the "B" binary toxin family include the Bacillus anthracis protective antigen (PA) protein,[3] most likely due to a common evolutionary ancestor. B. anthracis, a large Gram-positive spore-forming rod, is the causative agent of anthrax. Its two virulence factors are the poly-D-glutamate polypeptide capsule, and the actual anthrax exotoxin.[6] The toxin comprises three factors: the protective antigen (PA); the oedema factor (EF); and the lethal factor (LF). Each is a thermolabile protein of ~80kDa. PA forms the "B" part of the exotoxin and allows passage of the "A" moiety (consisting of EF and LF) into target cells. PA protein forms the central part of the complete anthrax toxin, and translocates the B moiety into host cells after assembling as a heptamer in the membrane.[6][7]

The AB5 toxins are usually considered a type of AB toxin, characterized by B pentamers. Less commonly, the term "AB toxin" is used to emphasize the monomeric character of the B component.

References[edit]

  1. ^ a b "Bacterial Pathogenesis: Bacterial Factors that Damage the Host - Producing Exotoxins - A-B Toxins". Retrieved 2008-12-13. 
  2. ^ De Haan L, Hirst TR (2004). "Cholera toxin: a paradigm for multi-functional engagement of cellular mechanisms (Review)". Mol. Membr. Biol. 21 (2): 77–92. doi:10.1080/09687680410001663267. PMID 15204437. 
  3. ^ a b c d Perelle S, Gibert M, Boquet P, Popoff MR (December 1993). "Characterization of Clostridium perfringens iota-toxin genes and expression in Escherichia coli". Infect. Immun. 61 (12): 5147–56. PMC 281295. PMID 8225592. 
  4. ^ a b c Fujii N, Kubota T, Shirakawa S, Kimura K, Ohishi I, Moriishi K, Isogai E, Isogai H (March 1996). "Characterization of component-I gene of botulinum C2 toxin and PCR detection of its gene in clostridial species". Biochem. Biophys. Res. Commun. 220 (2): 353–9. doi:10.1006/bbrc.1996.0409. PMID 8645309. 
  5. ^ a b c Stubbs S, Rupnik M, Gibert M, Brazier J, Duerden B, Popoff M (May 2000). "Production of actin-specific ADP-ribosyltransferase (binary toxin) by strains of Clostridium difficile". FEMS Microbiol. Lett. 186 (2): 307–12. PMID 10802189. 
  6. ^ a b Pezard C, Berche P, Mock M (October 1991). "Contribution of individual toxin components to virulence of Bacillus anthracis". Infect. Immun. 59 (10): 3472–7. PMC 258908. PMID 1910002. 
  7. ^ Welkos SL, Lowe JR, Eden-McCutchan F, Vodkin M, Leppla SH, Schmidt JJ (September 1988). "Sequence and analysis of the DNA encoding protective antigen of Bacillus anthracis". Gene 69 (2): 287–300. doi:10.1016/0378-1119(88)90439-8. PMID 3148491. 

This article incorporates text from the public domain Pfam and InterPro IPR003540

This article incorporates text from the public domain Pfam and InterPro IPR003896

This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.

This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Clostridial binary toxin B/anthrax toxin PA Provide feedback

The N-terminal region of this family contains a calcium-binding motif that may be an EF-hand.

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003896

A large group of bacterial exotoxins are referred to as "A/B toxins", essentially because they are formed from two subunits [PUBMED:8225592]. The "A" subunit possesses enzyme activity, and is transferred to the host cell following a conformational change in the membrane-bound transport "B" subunit. Clostridial species are one of the major causes of food poisoning/gastro-intestinal illnesses. They are Gram-positive, spore-forming rods that occur naturally in the soil [PUBMED:8225592]. Among the toxins produced by certain Clostridium spp. are the binary exotoxins. These proteins consist of two independent polypeptides, which correspond to the A/B subunit moieties. The enzyme component (A) enters the cell through endosomes produced by the oligomeric binding/translocation protein (B), and prevents actin polymerisation through ADP-ribosylation of monomeric G-actin [PUBMED:8225592, PUBMED:9659689, PUBMED:10802189].

Members of the "B" binary toxin family also include the Bacillus anthracis protective antigen (PA) protein [PUBMED:8225592], most likely due to a common evolutionary ancestor. B. anthracis, a large Gram-positive spore-forming rod, is the causative agent of anthrax. Its two virulence factors are the poly-D-glutamate polypeptide capsule, and the actual anthrax exotoxin [PUBMED:1910002]. The toxin comprises three factors: the protective antigen (PA); the oedema factor (EF); and the lethal factor (LF). Each is a thermolabile protein of ~80kDa. PA forms the "B" part of the exotoxin and allows passage of the "A" moiety (consisting of EF and LF) into target cells. PA protein forms the central part of the complete anthrax toxin, and translocates the B moiety into host cells after assembling as a heptamer in the membrane [PUBMED:1910002, PUBMED:3148491].

Gene Ontology

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Domain organisation

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Seed source: PRINTS
Previous IDs: none
Type: Family
Author: Griffiths-Jones SR
Number in seed: 8
Number in full: 100
Average length of the domain: 353.70 aa
Average identity of full alignment: 41 %
Average coverage of the sequence by the domain: 51.40 %

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HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 19.7 19.7
Trusted cut-off 19.8 19.9
Noise cut-off 17.8 19.6
Model length: 406
Family (HMM) version: 9
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Interactions

There are 2 interactions for this family. More...

Binary_toxB PA14

Structures

For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Binary_toxB domain has been found. There are 59 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.

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