1prt
From Proteopedia
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| - | [[Image:1prt.jpg|left|200px]] | + | [[Image:1prt.jpg|left|200px]] |
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| - | '''THE CRYSTAL STRUCTURE OF PERTUSSIS TOXIN''' | + | {{Structure |
| + | |PDB= 1prt |SIZE=350|CAPTION= <scene name='initialview01'>1prt</scene>, resolution 2.9Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''THE CRYSTAL STRUCTURE OF PERTUSSIS TOXIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PRT is a [ | + | 1PRT is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Bordetella_pertussis Bordetella pertussis]. The following page contains interesting information on the relation of 1PRT with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb69_1.html Cholera Toxin]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PRT OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8075982 8075982] |
[[Category: Bordetella pertussis]] | [[Category: Bordetella pertussis]] | ||
[[Category: Cholera Toxin]] | [[Category: Cholera Toxin]] | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:28:11 2008'' |
Revision as of 11:28, 20 March 2008
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| , resolution 2.9Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
THE CRYSTAL STRUCTURE OF PERTUSSIS TOXIN
Overview
BACKGROUND: Pertussis toxin is an exotoxin of the A-B class produced by Bordetella pertussis. The holotoxin comprises 952 residues forming six subunits (five different sequences, S1-S5). It plays an important role in the development of protective immunity to whooping cough, and is an essential component of new acellular vaccines. It is also widely used as a biochemical tool to ADP-ribosylate GTP-binding proteins in the study of signal transduction. RESULTS: The crystal structure of pertussis toxin has been determined at 2.9 A resolution. The catalytic A-subunit (S1) shares structural homology with other ADP-ribosylating bacterial toxins, although differences in the carboxy-terminal portion explain its unique activation mechanism. Despite its heterogeneous subunit composition, the structure of the cell-binding B-oligomer (S2, S3, two copies of S4, and S5) resembles the symmetrical B-pentamers of the cholera toxin and Shiga toxin families, but it interacts differently with the A-subunit. The structural similarity is all the more surprising given that there is almost no sequence homology between B-subunits of the different toxins. Two peripheral domains that are unique to the pertussis toxin B-oligomer show unexpected structural homology with a calcium-dependent eukaryotic lectin, and reveal possible receptor-binding sites. CONCLUSION: The structure provides insight into the pathogenic mechanisms of pertussis toxin and the evolution of bacterial toxins. Knowledge of the tertiary structure of the active site forms a rational basis for elimination of catalytic activity in recombinant molecules for vaccine use.
About this Structure
1PRT is a Protein complex structure of sequences from Bordetella pertussis. The following page contains interesting information on the relation of 1PRT with [Cholera Toxin]. Full crystallographic information is available from OCA.
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
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