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Contents |
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103 a.a.
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185 a.a.
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41 a.a.
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* Residue conservation analysis
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PDB id:
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Toxin
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Title:
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Refined structure of e. Coli heat labile enterotoxin, a close relative of cholera toxin
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Structure:
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Heat-labile enterotoxin, subunit b. Chain: d, e, f, g, h. Engineered: yes. Heat-labile enterotoxin, subunit a. Chain: a. Engineered: yes. Heat-labile enterotoxin, subunit a. Chain: c. Engineered: yes
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Source:
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Escherichia coli. Organism_taxid: 562. Cell_line: 293. Expressed in: escherichia coli. Expression_system_taxid: 562.
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Biol. unit:
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Heptamer (from
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Resolution:
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Authors:
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T.K.Sixma,W.G.J.Hol
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Key ref:
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T.K.Sixma
et al.
(1993).
Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin.
J Mol Biol,
230,
890-918.
PubMed id:
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Date:
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15-Jul-92
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Release date:
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31-Jan-94
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PROCHECK
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Headers
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References
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P32890
(ELBP_ECOLX) -
Heat-labile enterotoxin B chain from Escherichia coli
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Seq:
Struc:
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124 a.a.
103 a.a.
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J Mol Biol
230:890-918
(1993)
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PubMed id:
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Refined structure of Escherichia coli heat-labile enterotoxin, a close relative of cholera toxin.
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T.K.Sixma,
K.H.Kalk,
B.A.van Zanten,
Z.Dauter,
J.Kingma,
B.Witholt,
W.G.Hol.
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ABSTRACT
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Heat-labile enterotoxin (LT) from Escherichia coli is a bacterial protein toxin
with an AB5 multimer structure, in which the B pentamer has a membrane binding
function and the A subunit is needed for enzymatic activity. The LT crystal
structure has been solved using a combination of multiple isomorphous
replacement, fivefold averaging and molecular dynamics refinement. Phase
combination using all these sources of phase information was of crucial
importance for the chain tracing. The structure has now been refined to 1.95 A
resolution, resulting in a model containing 6035 protein atoms and 293 solvent
molecules with a crystallographic R-factor of 18.2% and good stereochemistry.
The B subunits are arranged as a highly stable pentamer with a donut shape. Each
subunit takes part in approximately 30 inter-subunit hydrogen bonds and six salt
bridges with its two neighbors, whilst burying a large surface area. The A
subunit has higher temperature factors and less well-defined secondary structure
than the B subunits. It interacts with the B pentamer mainly via the C-terminal
A2 fragment, which runs through the highly charged central pore of the B
subunits. The pore contains at least 66 water molecules, which fill the space
left by the A2 fragment. A detailed analysis of the contacts between A and B
subunits showed that most specific contacts occur at the entrance of the central
pore of the B pentamer, while the contacts within the pore are mainly
hydrophobic and water mediated, with the exception of two salt bridges. Only a
few contacts exist between the A1 fragment and the B pentamer, showing that the
A2 fragment functions as a "linker" of the A and B parts of the protein.
Interacting with the A subunit by the B subunits does not cause large deviations
from a common B subunit structure, and the 5-fold symmetry is well maintained. A
potential NAD(+)-binding site is located in an elongated crevice at the
interface of two small sheets in the A1 fragment. At the back of this crevice
the functionally important Arg7 makes a hydrogen bond connecting two strands,
which seems to be conserved across the ADP-ribosylating toxin family. The
putative catalytic residue (A1:Glu112) is located nearby, close to a very
hydrophobic region, which packs two loops together. This hydrophobic region may
be important for catalysis and membrane translocation.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.Burt,
C.Mallett,
M.Plante,
J.Zimmermann,
K.Torossian,
and
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(2011).
Proteosome-adjuvanted intranasal influenza vaccines: advantages, progress and future considerations.
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| |
Expert Rev Vaccines,
10,
365-375.
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F.Chowdhury,
Y.A.Begum,
M.M.Alam,
A.I.Khan,
T.Ahmed,
M.S.Bhuiyan,
J.B.Harris,
R.C.LaRocque,
A.S.Faruque,
H.Endtz,
E.T.Ryan,
A.Cravioto,
A.M.Svennerholm,
S.B.Calderwood,
and
F.Qadri
(2010).
Concomitant enterotoxigenic Escherichia coli infection induces increased immune responses to Vibrio cholerae O1 antigens in patients with cholera in Bangladesh.
|
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Infect Immun,
78,
2117-2124.
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P.M.Becker,
H.C.Widjaja-Greefkes,
and
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(2010).
Inhibition of binding of the AB5-type enterotoxins LT-I and cholera toxin to ganglioside GM1 by galactose-rich dietary components.
|
| |
Foodborne Pathog Dis,
7,
225-233.
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|
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|
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F.Qadri,
T.Ahmed,
F.Ahmed,
M.S.Bhuiyan,
M.G.Mostofa,
F.J.Cassels,
A.Helander,
and
A.M.Svennerholm
(2007).
Mucosal and systemic immune responses in patients with diarrhea due to CS6-expressing enterotoxigenic Escherichia coli.
|
| |
Infect Immun,
75,
2269-2274.
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|
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P.V.Alone,
G.Malik,
A.Krishnan,
and
L.C.Garg
(2007).
Deletion mutations in N-terminal alpha1 helix render heat labile enterotoxin B subunit susceptible to degradation.
|
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Proc Natl Acad Sci U S A,
104,
16056-16061.
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|
|
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T.D.Connell
(2007).
Cholera toxin, LT-I, LT-IIa and LT-IIb: the critical role of ganglioside binding in immunomodulation by type I and type II heat-labile enterotoxins.
|
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Expert Rev Vaccines,
6,
821-834.
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U.Baykal,
and
N.E.Tumer
(2007).
The C-terminus of pokeweed antiviral protein has distinct roles in transport to the cytosol, ribosome depurination and cytotoxicity.
|
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Plant J,
49,
995.
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F.Qadri,
F.Ahmed,
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and
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(2006).
Homologous and cross-reactive immune responses to enterotoxigenic Escherichia coli colonization factors in Bangladeshi children.
|
| |
Infect Immun,
74,
4512-4518.
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K.P.Holbourn,
C.C.Shone,
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(2006).
A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins.
|
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FEBS J,
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R.Stenutz,
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The structures of Escherichia coli O-polysaccharide antigens.
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Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
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| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
224-227.
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J.M.Mancheño,
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M.Martínez-Ripoll,
and
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Structural analysis of the Laetiporus sulphureus hemolytic pore-forming lectin in complex with sugars.
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| |
J Biol Chem,
280,
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PDB codes:
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A.Holmner,
M.Lebens,
S.Teneberg,
J.Angström,
M.Okvist,
and
U.Krengel
(2004).
Novel binding site identified in a hybrid between cholera toxin and heat-labile enterotoxin: 1.9 A crystal structure reveals the details.
|
| |
Structure,
12,
1655-1667.
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|
PDB codes:
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A.L.Horstman,
S.J.Bauman,
and
M.J.Kuehn
(2004).
Lipopolysaccharide 3-deoxy-D-manno-octulosonic acid (Kdo) core determines bacterial association of secreted toxins.
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J Biol Chem,
279,
8070-8075.
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J.Sun,
A.W.Maresso,
J.J.Kim,
and
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(2004).
How bacterial ADP-ribosylating toxins recognize substrates.
|
| |
Nat Struct Mol Biol,
11,
868-876.
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M.Apostolaki,
and
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(2004).
Nasal delivery of antigen with the B subunit of Escherichia coli heat-labile enterotoxin augments antigen-specific T-cell clonal expansion and differentiation.
|
| |
Infect Immun,
72,
4072-4080.
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J.K.Tinker,
J.L.Erbe,
W.G.Hol,
and
R.K.Holmes
(2003).
Cholera holotoxin assembly requires a hydrophobic domain at the A-B5 interface: mutational analysis and development of an in vitro assembly system.
|
| |
Infect Immun,
71,
4093-4101.
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|
|
|
|
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Y.Fujinaga,
A.A.Wolf,
C.Rodighiero,
H.Wheeler,
B.Tsai,
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T.Rapoport,
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and
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(2003).
Gangliosides that associate with lipid rafts mediate transport of cholera and related toxins from the plasma membrane to endoplasmic reticulm.
|
| |
Mol Biol Cell,
14,
4783-4793.
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|
|
|
|
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A.L.Horstman,
and
M.J.Kuehn
(2002).
Bacterial surface association of heat-labile enterotoxin through lipopolysaccharide after secretion via the general secretory pathway.
|
| |
J Biol Chem,
277,
32538-32545.
|
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C.A.Menezes,
J.Amianti,
H.S.Harayama,
P.C.Koga,
L.R.Trabulsi,
and
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(2002).
Inhibition of Escherichia coli heat-labile enterotoxin by neoglycoprotein and anti-lectin antibodies which mimic GM1 receptor.
|
| |
FEMS Microbiol Lett,
216,
67-70.
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C.Lesieur,
M.J.Cliff,
R.Carter,
R.F.James,
A.R.Clarke,
and
T.R.Hirst
(2002).
A kinetic model of intermediate formation during assembly of cholera toxin B-subunit pentamers.
|
| |
J Biol Chem,
277,
16697-16704.
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|
|
|
|
|
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M.G.Jobling,
and
R.K.Holmes
(2002).
Mutational analysis of ganglioside GM(1)-binding ability, pentamer formation, and epitopes of cholera toxin B (CTB) subunits and CTB/heat-labile enterotoxin B subunit chimeras.
|
| |
Infect Immun,
70,
1260-1271.
|
|
|
|
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|
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R.Bhattacharyya,
D.Pal,
and
P.Chakrabarti
(2002).
Secondary structures at polypeptide-chain termini and their features.
|
| |
Acta Crystallogr D Biol Crystallogr,
58,
1793-1802.
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R.Glück
(2002).
Intranasal immunization against influenza.
|
| |
J Aerosol Med,
15,
221-228.
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A.T.Aman,
S.Fraser,
E.A.Merritt,
C.Rodigherio,
M.Kenny,
M.Ahn,
W.G.Hol,
N.A.Williams,
W.I.Lencer,
and
T.R.Hirst
(2001).
A mutant cholera toxin B subunit that binds GM1- ganglioside but lacks immunomodulatory or toxic activity.
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Proc Natl Acad Sci U S A,
98,
8536-8541.
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PDB code:
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E.Fan,
E.A.Merritt,
Z.Zhang,
J.C.Pickens,
C.Roach,
M.Ahn,
and
W.G.Hol
(2001).
Exploration of the GM1 receptor-binding site of heat-labile enterotoxin and cholera toxin by phenyl-ring-containing galactose derivatives.
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Acta Crystallogr D Biol Crystallogr,
57,
201-212.
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PDB codes:
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M.E.Scott,
Z.Y.Dossani,
and
M.Sandkvist
(2001).
Directed polar secretion of protease from single cells of Vibrio cholerae via the type II secretion pathway.
|
| |
Proc Natl Acad Sci U S A,
98,
13978-13983.
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|
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M.G.Jobling,
and
R.K.Holmes
(2001).
Biological and biochemical characterization of variant A subunits of cholera toxin constructed by site-directed mutagenesis.
|
| |
J Bacteriol,
183,
4024-4032.
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S.Wimer-Mackin,
R.K.Holmes,
A.A.Wolf,
W.I.Lencer,
and
M.G.Jobling
(2001).
Characterization of receptor-mediated signal transduction by Escherichia coli type IIa heat-labile enterotoxin in the polarized human intestinal cell line T84.
|
| |
Infect Immun,
69,
7205-7212.
|
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X.Zhu,
E.Kim,
A.L.Boman,
A.Hodel,
W.Cieplak,
and
R.A.Kahn
(2001).
ARF binds the C-terminal region of the Escherichia coli heat-labile toxin (LTA1) and competes for the binding of LTA2.
|
| |
Biochemistry,
40,
4560-4568.
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|
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E.Fan,
E.A.Merritt,
C.L.Verlinde,
and
W.G.Hol
(2000).
AB(5) toxins: structures and inhibitor design.
|
| |
Curr Opin Struct Biol,
10,
680-686.
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J.Humbert,
M.Jouve,
C.Le Bouguénec,
and
P.Gounon
(2000).
Electron microscopic improvement in the study of diarrheagenic Escherichia coli.
|
| |
Microsc Res Tech,
49,
383-393.
|
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K.M.Dolan,
G.Lindenmayer,
and
J.C.Olson
(2000).
Functional comparison of the NAD binding cleft of ADP-ribosylating toxins.
|
| |
Biochemistry,
39,
8266-8275.
|
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|
|
|
|
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M.G.Jobling,
and
R.K.Holmes
(2000).
Identification of motifs in cholera toxin A1 polypeptide that are required for its interaction with human ADP-ribosylation factor 6 in a bacterial two-hybrid system.
|
| |
Proc Natl Acad Sci U S A,
97,
14662-14667.
|
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M.Nagahama,
Y.Sakaguchi,
K.Kobayashi,
S.Ochi,
and
J.Sakurai
(2000).
Characterization of the enzymatic component of Clostridium perfringens iota-toxin.
|
| |
J Bacteriol,
182,
2096-2103.
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S.Swaminathan,
and
S.Eswaramoorthy
(2000).
Crystallization and preliminary X-ray analysis of Clostridium botulinum neurotoxin type B.
|
| |
Acta Crystallogr D Biol Crystallogr,
56,
1024-1026.
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W.E.Minke,
J.Pickens,
E.A.Merritt,
E.Fan,
C.L.Verlinde,
and
W.G.Hol
(2000).
Structure of m-carboxyphenyl-alpha-D-galactopyranoside complexed to heat-labile enterotoxin at 1.3 A resolution: surprising variations in ligand-binding modes.
|
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Acta Crystallogr D Biol Crystallogr,
56,
795-804.
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PDB code:
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Y.Matsushima-Hibiya,
M.Watanabe,
T.Kono,
T.Kanazawa,
K.Koyama,
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(2000).
Purification and cloning of pierisin-2, an apoptosis-inducing protein from the cabbage butterfly, Pieris brassicae.
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C.Rodighiero,
A.T.Aman,
M.J.Kenny,
J.Moss,
W.I.Lencer,
and
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(1999).
Structural basis for the differential toxicity of cholera toxin and Escherichia coli heat-labile enterotoxin. Construction of hybrid toxins identifies the A2-domain as the determinant of differential toxicity.
|
| |
J Biol Chem,
274,
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|
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|
D.Matković-Calogović,
A.Loregian,
M.R.D'Acunto,
R.Battistutta,
A.Tossi,
G.Palù,
and
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(1999).
Crystal structure of the B subunit of Escherichia coli heat-labile enterotoxin carrying peptides with anti-herpes simplex virus type 1 activity.
|
| |
J Biol Chem,
274,
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|
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PDB codes:
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|
|
E.Cheng,
L.Cárdenas-Freytag,
and
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(1999).
The role of cAMP in mucosal adjuvanticity of Escherichia coli heat-labile enterotoxin (LT).
|
| |
Vaccine,
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(1999).
Characterization of glycosylphosphatidylinositiol-anchored, secreted, and intracellular vertebrate mono-ADP-ribosyltransferases.
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Annu Rev Nutr,
19,
485-509.
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M.Watanabe,
T.Kono,
Y.Matsushima-Hibiya,
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N.Nishisaka,
T.Kishimoto,
K.Koyama,
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(1999).
Molecular cloning of an apoptosis-inducing protein, pierisin, from cabbage butterfly: possible involvement of ADP-ribosylation in its activity.
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Proc Natl Acad Sci U S A,
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N.Le Novère,
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(1999).
Improved secondary structure predictions for a nicotinic receptor subunit: incorporation of solvent accessibility and experimental data into a two-dimensional representation.
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| |
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W.E.Minke,
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(1999).
Structure-based exploration of the ganglioside GM1 binding sites of Escherichia coli heat-labile enterotoxin and cholera toxin for the discovery of receptor antagonists.
|
| |
Biochemistry,
38,
5684-5692.
|
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A.Ruf,
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and
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(1998).
Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling.
|
| |
Biochemistry,
37,
3893-3900.
|
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PDB codes:
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|
G.Del Giudice,
M.Pizza,
and
R.Rappuoli
(1998).
Molecular basis of vaccination.
|
| |
Mol Aspects Med,
19,
1.
|
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I.J.Okazaki,
and
J.Moss
(1998).
Glycosylphosphatidylinositol-anchored and secretory isoforms of mono-ADP-ribosyltransferases.
|
| |
J Biol Chem,
273,
23617-23620.
|
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J.P.Nataro,
and
J.B.Kaper
(1998).
Diarrheagenic Escherichia coli.
|
| |
Clin Microbiol Rev,
11,
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|
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J.P.Thompson,
and
C.L.Schengrund
(1998).
Inhibition of the adherence of cholera toxin and the heat-labile enterotoxin of Escherichia coli to cell-surface GM1 by oligosaccharide-derivatized dendrimers.
|
| |
Biochem Pharmacol,
56,
591-597.
|
|
|
|
|
|
|
K.Okamoto,
T.Nomura,
Y.Fujii,
and
H.Yamanaka
(1998).
Contribution of the disulfide bond of the A subunit to the action of Escherichia coli heat-labile enterotoxin.
|
| |
J Bacteriol,
180,
1368-1374.
|
|
|
|
|
|
|
L.Agren,
B.Löwenadler,
and
N.Lycke
(1998).
A novel concept in mucosal adjuvanticity: the CTA1-DD adjuvant is a B cell-targeted fusion protein that incorporates the enzymatically active cholera toxin A1 subunit.
|
| |
Immunol Cell Biol,
76,
280-287.
|
|
|
|
|
|
|
M.M.Giuliani,
G.Del Giudice,
V.Giannelli,
G.Dougan,
G.Douce,
R.Rappuoli,
and
M.Pizza
(1998).
Mucosal adjuvanticity and immunogenicity of LTR72, a novel mutant of Escherichia coli heat-labile enterotoxin with partial knockout of ADP-ribosyltransferase activity.
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PDB code:
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Protein Sci,
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(1996).
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Biochemistry,
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PDB code:
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Infect Immun,
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Crystal structure of a new heat-labile enterotoxin, LT-IIb.
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Structure,
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PDB code:
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I.K.Feil,
R.Reddy,
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Protein engineering studies of A-chain loop 47-56 of Escherichia coli heat-labile enterotoxin point to a prominent role of this loop for cytotoxicity.
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Mol Microbiol,
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A pH-dependent conformational change in the B-subunit pentamer of Escherichia coli heat-labile enterotoxin: structural basis and possible functional role for a conserved feature of the AB5 toxin family.
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Biochemistry,
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Assembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Kinetics and molecular basis of rate-limiting steps in vitro.
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J Biol Chem,
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Infect Immun,
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Eur J Biochem,
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E.A.Merritt,
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| |
Nat Struct Biol,
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PDB code:
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E.A.Merritt,
and
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Kinetics of acid-mediated disassembly of the B subunit pentamer of Escherichia coli heat-labile enterotoxin. Molecular basis of pH stability.
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J Biol Chem,
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Formation of ion channels in lipid bilayers by a peptide with the predicted transmembrane sequence of botulinum neurotoxin A.
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Generation of a monoclonal antibody that recognizes the amino-terminal decapeptide of the B-subunit of Escherichia coli heat-labile enterotoxin. A new probe for studying toxin assembly intermediates.
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PDB code:
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Mol Microbiol,
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Probing the structure-activity relationship of Escherichia coli LT-A by site-directed mutagenesis.
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Mol Microbiol,
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The crystal structure of pertussis toxin.
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| |
Structure,
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PDB code:
|
|
|
|
|
|
|
|
W.N.Burnette
(1994).
AB5 ADP-ribosylating toxins: comparative anatomy and physiology.
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| |
Structure,
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|
|
The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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