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{{STRUCTURE_1tii|  PDB=1tii  |  SCENE=  }}  
{{STRUCTURE_1tii|  PDB=1tii  |  SCENE=  }}  


'''ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB'''
===ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB===




==Overview==
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BACKGROUND: Cholera toxin from Vibrio cholerae and the type I heat-labile enterotoxins (LT-Is) from Escherichia coli are oligomeric proteins with AB5 structures. The type II heat-labile enterotoxins (LT-IIs) from E. coli are structurally similar to, but antigenically distinct from, the type I enterotoxins. The A subunits of type I and type II enterotoxins are homologous and activate adenylate cyclase by ADP-ribosylation of a G protein subunit, G8 alpha. However, the B subunits of type I and type II enterotoxins differ dramatically in amino acid sequence and ganglioside-binding specificity. The structure of LT-IIb was determined both as a prototype for other LT-IIs and to provide additional insights into structure/function relationships among members of the heat-labile enterotoxin family and the superfamily of ADP-ribosylating protein toxins. RESULTS: The 2.25 A crystal structure of the LT-IIb holotoxin has been determined. The structure reveals striking similarities with LT-I in both the catalytic A subunit and the ganglioside-binding B subunits. The latter form a pentamer which has a central pore with a diameter of 10-18 A. Despite their similarities, the relative orientation between the A polypeptide and the B pentamer differs by 24 degrees in LT-I and LT-IIb. A common hydrophobic ring was observed at the A-B5 interface which may be important in the cholera toxin family for assembly of the AB5 heterohexamer. A cluster of arginine residues at the surface of the A subunit of LT-I and cholera toxin, possibly involved in assembly, is also present in LT-IIb. The ganglioside receptor binding sites are localized, as suggested by mutagenesis, and are in a position roughly similar to the sites where LT-I binds its receptor. CONCLUSIONS: The structure of LT-IIb provides insight into the sequence diversity and structural similarity of the AB5 toxin family. New knowledge has been gained regarding the assembly of AB5 toxins and their active-site architecture.
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==About this Structure==
==About this Structure==
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[[Category: Enterotoxin]]
[[Category: Enterotoxin]]
[[Category: Ganglioside receptor]]
[[Category: Ganglioside receptor]]
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Revision as of 01:55, 29 July 2008

File:1tii.png

Template:STRUCTURE 1tii

ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB

Template:ABSTRACT PUBMED 8805549

About this Structure

1TII is a Protein complex structure of sequences from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Crystal structure of a new heat-labile enterotoxin, LT-IIb., van den Akker F, Sarfaty S, Twiddy EM, Connell TD, Holmes RK, Hol WG, Structure. 1996 Jun 15;4(6):665-78. PMID:8805549

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