1prt
From Proteopedia
(New page: 200px<br /> <applet load="1prt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1prt, resolution 2.9Å" /> '''THE CRYSTAL STRUCTUR...) |
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caption="1prt, resolution 2.9Å" /> | caption="1prt, resolution 2.9Å" /> | ||
'''THE CRYSTAL STRUCTURE OF PERTUSSIS TOXIN'''<br /> | '''THE CRYSTAL STRUCTURE OF PERTUSSIS TOXIN'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PRT is a [http://en.wikipedia.org/wiki/Protein_complex 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:// | + | 1PRT is a [http://en.wikipedia.org/wiki/Protein_complex 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== | ||
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[[Category: toxin]] | [[Category: toxin]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:41:12 2008'' |
Revision as of 14:41, 15 February 2008
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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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