1tii
From Proteopedia
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| - | [[Image:1tii.jpg|left|200px]] | + | [[Image:1tii.jpg|left|200px]] |
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| - | '''ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB''' | + | {{Structure |
| + | |PDB= 1tii |SIZE=350|CAPTION= <scene name='initialview01'>1tii</scene>, resolution 2.25Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TII is a [ | + | 1TII is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TII OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8805549 8805549] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: ganglioside receptor]] | [[Category: ganglioside receptor]] | ||
| - | ''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 14:18:49 2008'' |
Revision as of 12:18, 20 March 2008
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ESCHERICHIA COLI HEAT LABILE ENTEROTOXIN TYPE IIB
Overview
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.
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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