1PRT | Toxin | date | Nov 22, 1993 ![]() ![]() |
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title | The Crystal Structure Of Pertussis Toxin | ||||||||||||||||||
authors | P.E.Stein, R.J.Read | ||||||||||||||||||
compound | source | ||||||||||||||||||
Molecule: Pertussis Toxin (Subunit S1) Chain: A, G Engineered: Yes |
Organism_scientific: Bordetella Pertussis | ||||||||||||||||||
Molecule: Pertussis Toxin (Subunit S2) Chain: B, H Engineered: Yes |
Organism_scientific: Bordetella Pertussis | ||||||||||||||||||
Molecule: Pertussis Toxin (Subunit S3) Chain: C, I Engineered: Yes |
Organism_scientific: Bordetella Pertussis | ||||||||||||||||||
Molecule: Pertussis Toxin (Subunit S4) Chain: D, E, J, K Engineered: Yes |
Organism_scientific: Bordetella Pertussis | ||||||||||||||||||
Molecule: Pertussis Toxin (Subunit S5) Chain: F, L Engineered: Yes |
Organism_scientific: Bordetella Pertussis | ||||||||||||||||||
symmetry | Space Group: P 21 21 21 | R_factor | 0.195 | ||||||||||||||||
crystal cell |
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method | X-Ray Diffraction | resolution | 2.90 Å | ||||||||||||||||
note | 1PRT (Molecule of the Month:pdb69) | ||||||||||||||||||
related structures | by homologous chain: 1BCP | ||||||||||||||||||
domain | The region which spans amino-acids 42-49 is required for enzymatic activity and contributes to the formation of a potentially important antigenic determinant. | ||||||||||||||||||
similarity | Belongs to the pertussis toxin s2/s3 subunits family.[Pertussis_S1] | ||||||||||||||||||
subunit | Pertussis toxin contains five different chains, s1-s5. They are organized into 2 functional subunits: a, composed of s1 (which is toxic) and b, containing s2, s3, s5, and two copies of s4 (b binds to the membrane receptors). Dimers of s2-s4 and s3-s4 are held together by s5. | ||||||||||||||||||
Genes | BP3783, BP3784, BP3785, BP3786, BP3787, PTXA, PTXB, PTXC, PTXD, PTXE (B. pertussis) | ||||||||||||||||||
function | In the absence of g proteins it also catalyzes the cleavage of nad(+) into adp-ribose and nicotinamide. Ptx oligomer b binds to receptors on the eukaryotic cell surface and facilitates the translocation of the toxic subunit across the cell membrane. It catalyzes the adp-ribosylation of a cysteine in the alpha subunit of heterotrimeric g proteins. It irreversibly uncouples the g-alpha gtp-binding proteins from their membrane receptors. S1 is an nad-dependent adp-ribosyltransferase. | ||||||||||||||||||
Gene Ontology |
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Primary reference | The crystal structure of pertussis toxin., Stein PE, Boodhoo A, Armstrong GD, Cockle SA, Klein MH, Read RJ, Structure 1994 Jan 15;2(1):45-57. PMID:8075982 |
Data retrieval |
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Structure-derived information |
- Domain d1prta_, region A [Jmol] [rasmolscript] [script source] - Domain d1prtb2, region B:4-89 [Jmol] [rasmolscript] [script source] - Domain d1prtb1, region B:90-199 [Jmol] [rasmolscript] [script source] - Domain d1prtc2, region C:4-89 [Jmol] [rasmolscript] [script source] - Domain d1prtc1, region C:90-199 [Jmol] [rasmolscript] [script source] - Domain d1prtd_, region D [Jmol] [rasmolscript] [script source] - Domain d1prte_, region E [Jmol] [rasmolscript] [script source] - Domain d1prtf_, region F [Jmol] [rasmolscript] [script source] - Domain d1prtg_, region G [Jmol] [rasmolscript] [script source] - Domain d1prth2, region H:4-89 [Jmol] [rasmolscript] [script source] - Domain d1prth1, region H:90-199 [Jmol] [rasmolscript] [script source] - Domain d1prti2, region I:4-89 [Jmol] [rasmolscript] [script source] - Domain d1prti1, region I:90-199 [Jmol] [rasmolscript] [script source] - Domain d1prtj_, region J [Jmol] [rasmolscript] [script source] - Domain d1prtk_, region K [Jmol] [rasmolscript] [script source] - Domain d1prtl_, region L [Jmol] [rasmolscript] [script source] |
Sequence-derived information |
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