|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
224 a.a.
|
|
|
|
|
|
|
|
|
|
|
196 a.a.
|
|
|
|
|
|
|
|
|
|
|
196 a.a.
|
|
|
|
|
|
|
|
|
|
|
110 a.a.
|
|
|
|
|
|
|
|
|
|
|
98 a.a.
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
PDB id:
|
|
|
|
| Name: |
|
Toxin
|
|
|
Title:
|
|
The crystal structure of pertussis toxin
|
|
Structure:
|
|
Pertussis toxin (subunit s1). Chain: a, g. Engineered: yes. Pertussis toxin (subunit s2). Chain: b, h. Engineered: yes. Pertussis toxin (subunit s3). Chain: c, i. Engineered: yes.
|
|
Source:
|
|
Bordetella pertussis. Organism_taxid: 520. Organism_taxid: 520
|
|
Biol. unit:
|
|
Hexamer (from
)
|
|
Resolution:
|
|
|
|
Authors:
|
|
P.E.Stein,R.J.Read
|
Key ref:
|
|
P.E.Stein
et al.
(1994).
The crystal structure of pertussis toxin.
Structure,
2,
45-57.
PubMed id:
DOI:
|
|
|
Date:
|
|
|
22-Nov-93
|
Release date:
|
26-Jan-95
|
|
|
|
|
|
|
PROCHECK
|
|
|
|
|
|
Headers
|
|
|
|
References
|
|
|
|
|
|
|
|
P04977
(TOX1_BORPE) -
Pertussis toxin subunit 1 from Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
|
|
|
|
Seq:
Struc:
|
|
|
|
269 a.a.
224 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P04978
(TOX2_BORPE) -
Pertussis toxin subunit 2 from Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
|
|
|
|
Seq:
Struc:
|
|
|
|
226 a.a.
196 a.a.*
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
P04979
(TOX3_BORPE) -
Pertussis toxin subunit 3 from Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
|
|
|
|
Seq:
Struc:
|
|
|
|
227 a.a.
196 a.a.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Structure
2:45-57
(1994)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
The crystal structure of pertussis toxin.
|
|
P.E.Stein,
A.Boodhoo,
G.D.Armstrong,
S.A.Cockle,
M.H.Klein,
R.J.Read.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
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.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 2.
Figure 2. Stereo views of Cα representations of individual
pertussis toxin subunits, in the same orientation as Figure 1a.
(a)S1, (b)S2, (c)S4, and (d)S5. S3, which is very similar to S2,
is not shown. The amino (N) and carboxyl (C) termini of each
subunit are labelled and the Cα atom of every tenth residue is
numbered. Secondary structure was assigned with DSSP [55]. S1 β
1, 6–11; α1, 15–21; β2, 23–24; α2, 32–37; β3,
50–54; α3, 57–77; β4, 83–92; β5, 97–99, α4,
100–111; α5, 118–127; β6, 129–133; β7, 135–136; β8,
141–150; β9, 155–162; β10, 191–193; β11, 198–199;
α6, 200–205; β12; 225–227; α7, 228–231. S2 and S3
amino-terminal domain: β 1, 27–29; α1, 32–37; α2,
39–48; β2, 54–56; β3, 61–63; β4, 70–72; β5, 84–93.
Carboxy-terminal domain: β6, 100–105; β7, 106–113; β8,
119–125; β9, 128–135; α3, 146–159; β10, 163–173;
β11, 183–191. S4: β1, 6–10; β2, 11–20; β3, 27–36;
β4, 48–55; α1, 63–74; β5, 78–89; β6, 92–102. S5:
β1, 5– 9; β2, 10–20; β3, 23–31; β4, 37–43; α1,
51– 66; β5, 70–74; β6, 84–91. Figure 2. Stereo views
of Cα representations of individual pertussis toxin subunits,
in the same orientation as Figure 1a. (a)S1, (b)S2, (c)S4, and
(d)S5. S3, which is very similar to S2, is not shown. The amino
(N) and carboxyl (C) termini of each subunit are labelled and
the Cα atom of every tenth residue is numbered. Secondary
structure was assigned with DSSP [[4]55]. S1 β 1, 6–11; α1,
15–21; β2, 23–24; α2, 32–37; β3, 50–54; α3, 57–77;
β4, 83–92; β5, 97–99, α4, 100–111; α5, 118–127; β6,
129–133; β7, 135–136; β8, 141–150; β9, 155–162; β10,
191–193; β11, 198–199; α6, 200–205; β12; 225–227;
α7, 228–231. S2 and S3 amino-terminal domain: β 1, 27–29;
α1, 32–37; α2, 39–48; β2, 54–56; β3, 61–63; β4,
70–72; β5, 84–93. Carboxy-terminal domain: β6, 100–105;
β7, 106–113; β8, 119–125; β9, 128–135; α3, 146–159;
β10, 163–173; β11, 183–191. S4: β1, 6–10; β2, 11–20;
β3, 27–36; β4, 48–55; α1, 63–74; β5, 78–89; β6,
92–102. S5: β1, 5– 9; β2, 10–20; β3, 23–31; β4,
37–43; α1, 51– 66; β5, 70–74; β6, 84–91.
|
|
Figure 3.
Figure 3. Stereo view of Cα tracings of PT (blue) and LT (red)
with their A-subunits superimposed. Figure 3. Stereo view of
Cα tracings of PT (blue) and LT (red) with their A-subunits
superimposed.
|
|
|
|
|
|
| |
The above figures are
reprinted
by permission from Cell Press:
Structure
(1994,
2,
45-57)
copyright 1994.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
N.H.Carbonetti
(2010).
Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology tools.
|
| |
Future Microbiol,
5,
455-469.
|
|
|
|
|
|
|
R.S.Sedeh,
M.Bathe,
and
K.J.Bathe
(2010).
The subspace iteration method in protein normal mode analysis.
|
| |
J Comput Chem,
31,
66-74.
|
|
|
|
|
|
|
A.A.Aksyuk,
P.G.Leiman,
L.P.Kurochkina,
M.M.Shneider,
V.A.Kostyuchenko,
V.V.Mesyanzhinov,
and
M.G.Rossmann
(2009).
The tail sheath structure of bacteriophage T4: a molecular machine for infecting bacteria.
|
| |
EMBO J,
28,
821-829.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
B.Heras,
S.R.Shouldice,
M.Totsika,
M.J.Scanlon,
M.A.Schembri,
and
J.L.Martin
(2009).
DSB proteins and bacterial pathogenicity.
|
| |
Nat Rev Microbiol,
7,
215-225.
|
|
|
|
|
|
|
E.M.Warren,
H.Huang,
E.Fanning,
W.J.Chazin,
and
B.F.Eichman
(2009).
Physical interactions between Mcm10, DNA, and DNA polymerase alpha.
|
| |
J Biol Chem,
284,
24662-24672.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
J.N.Sutherland,
and
J.A.Maynard
(2009).
Characterization of a key neutralizing epitope on pertussis toxin recognized by monoclonal antibody 1B7.
|
| |
Biochemistry,
48,
11982-11993.
|
|
|
|
|
|
|
P.W.Dunten,
E.J.Little,
and
N.C.Horton
(2009).
The restriction enzyme SgrAI: structure solution via combination of poor MIRAS and MR phases.
|
| |
Acta Crystallogr D Biol Crystallogr,
65,
393-398.
|
|
|
|
|
|
|
D.Bose,
T.Pape,
P.C.Burrows,
M.Rappas,
S.R.Wigneshweraraj,
M.Buck,
and
X.Zhang
(2008).
Organization of an activator-bound RNA polymerase holoenzyme.
|
| |
Mol Cell,
32,
337-346.
|
|
|
|
|
|
|
R.D.Plaut,
and
N.H.Carbonetti
(2008).
Retrograde transport of pertussis toxin in the mammalian cell.
|
| |
Cell Microbiol,
10,
1130-1139.
|
|
|
|
|
|
|
R.S.Ampapathi,
A.L.Creath,
D.I.Lou,
J.W.Craft,
S.R.Blanke,
and
G.B.Legge
(2008).
Order-disorder-order transitions mediate the activation of cholera toxin.
|
| |
J Mol Biol,
377,
748-760.
|
|
|
|
|
|
|
S.Farrand,
E.Hotze,
P.Friese,
S.K.Hollingshead,
D.F.Smith,
R.D.Cummings,
G.L.Dale,
and
R.K.Tweten
(2008).
Characterization of a streptococcal cholesterol-dependent cytolysin with a lewis y and b specific lectin domain.
|
| |
Biochemistry,
47,
7097-7107.
|
|
|
|
|
|
|
A.Verma,
and
D.L.Burns
(2007).
Requirements for assembly of PtlH with the pertussis toxin transporter apparatus of Bordetella pertussis.
|
| |
Infect Immun,
75,
2297-2306.
|
|
|
|
|
|
|
D.H.Anderson,
V.A.Kickhoefer,
S.A.Sievers,
L.H.Rome,
and
D.Eisenberg
(2007).
Draft crystal structure of the vault shell at 9-A resolution.
|
| |
PLoS Biol,
5,
e318.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
R.F.Collins,
M.Saleem,
and
J.P.Derrick
(2007).
Purification and three-dimensional electron microscopy structure of the Neisseria meningitidis type IV pilus biogenesis protein PilG.
|
| |
J Bacteriol,
189,
6389-6396.
|
|
|
|
|
|
|
Z.E.Worthington,
and
N.H.Carbonetti
(2007).
Evading the proteasome: absence of lysine residues contributes to pertussis toxin activity by evasion of proteasome degradation.
|
| |
Infect Immun,
75,
2946-2953.
|
|
|
|
|
|
|
A.H.Pande,
D.Moe,
M.Jamnadas,
S.A.Tatulian,
and
K.Teter
(2006).
The pertussis toxin S1 subunit is a thermally unstable protein susceptible to degradation by the 20S proteasome.
|
| |
Biochemistry,
45,
13734-13740.
|
|
|
|
|
|
|
D.Raze,
A.Veithen,
H.Sato,
R.Antoine,
F.D.Menozzi,
and
C.Locht
(2006).
Genetic exchange of the S2 and S3 subunits in pertussis toxin.
|
| |
Mol Microbiol,
60,
1241-1250.
|
|
|
|
|
|
|
K.P.Holbourn,
C.C.Shone,
and
K.R.Acharya
(2006).
A family of killer toxins. Exploring the mechanism of ADP-ribosylating toxins.
|
| |
FEBS J,
273,
4579-4593.
|
|
|
|
|
|
|
S.Kernstock,
F.Koch-Nolte,
J.Mueller-Dieckmann,
M.S.Weiss,
and
C.Mueller-Dieckmann
(2006).
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
62,
224-227.
|
|
|
|
|
|
|
A.N.Zelensky,
and
J.E.Gready
(2005).
The C-type lectin-like domain superfamily.
|
| |
FEBS J,
272,
6179-6217.
|
|
|
|
|
|
|
B.Chen,
E.M.Vogan,
H.Gong,
J.J.Skehel,
D.C.Wiley,
and
S.C.Harrison
(2005).
Determining the structure of an unliganded and fully glycosylated SIV gp120 envelope glycoprotein.
|
| |
Structure,
13,
197-211.
|
|
|
|
|
|
|
N.H.Carbonetti,
R.M.Mays,
G.V.Artamonova,
R.D.Plaut,
and
Z.E.Worthington
(2005).
Proteolytic cleavage of pertussis toxin S1 subunit is not essential for its activity in mammalian cells.
|
| |
BMC Microbiol,
5,
7.
|
|
|
|
|
|
|
R.F.Collins,
S.A.Frye,
S.Balasingham,
R.C.Ford,
T.Tønjum,
and
J.P.Derrick
(2005).
Interaction with type IV pili induces structural changes in the bacterial outer membrane secretin PilQ.
|
| |
J Biol Chem,
280,
18923-18930.
|
|
|
|
|
|
|
A.M.Cheung,
K.M.Farizo,
and
D.L.Burns
(2004).
Analysis of relative levels of production of pertussis toxin subunits and Ptl proteins in Bordetella pertussis.
|
| |
Infect Immun,
72,
2057-2066.
|
|
|
|
|
|
|
D.L.Burns,
S.Fiddner,
A.M.Cheung,
and
A.Verma
(2004).
Analysis of subassemblies of pertussis toxin subunits in vivo and their interaction with the ptl transport apparatus.
|
| |
Infect Immun,
72,
5365-5372.
|
|
|
|
|
|
|
F.Dong,
J.Sharma,
Y.Xiao,
Y.Zhong,
and
G.Zhong
(2004).
Intramolecular dimerization is required for the chlamydia-secreted protease CPAF to degrade host transcriptional factors.
|
| |
Infect Immun,
72,
3869-3875.
|
|
|
|
|
|
|
F.Dong,
M.Pirbhai,
Y.Zhong,
and
G.Zhong
(2004).
Cleavage-dependent activation of a chlamydia-secreted protease.
|
| |
Mol Microbiol,
52,
1487-1494.
|
|
|
|
|
|
|
H.Barth,
K.Aktories,
M.R.Popoff,
and
B.G.Stiles
(2004).
Binary bacterial toxins: biochemistry, biology, and applications of common Clostridium and Bacillus proteins.
|
| |
Microbiol Mol Biol Rev,
68,
373.
|
|
|
|
|
|
|
H.J.Yeo,
and
G.Waksman
(2004).
Unveiling molecular scaffolds of the type IV secretion system.
|
| |
J Bacteriol,
186,
1919-1926.
|
|
|
|
|
|
|
H.Remaut,
and
G.Waksman
(2004).
Structural biology of bacterial pathogenesis.
|
| |
Curr Opin Struct Biol,
14,
161-170.
|
|
|
|
|
|
|
J.Sun,
A.W.Maresso,
J.J.Kim,
and
J.T.Barbieri
(2004).
How bacterial ADP-ribosylating toxins recognize substrates.
|
| |
Nat Struct Mol Biol,
11,
868-876.
|
|
|
|
|
|
|
K.Kamachi,
and
Y.Arakawa
(2004).
Expression of a C terminally truncated form of pertussis toxin S1 subunit effectively induces protection against pertussis toxin following DNA-based immunization.
|
| |
Infect Immun,
72,
4293-4296.
|
|
|
|
|
|
|
M.D.Feese,
T.Tamada,
Y.Kato,
Y.Maeda,
M.Hirose,
Y.Matsukura,
H.Shigematsu,
T.Muto,
A.Matsumoto,
H.Watarai,
K.Ogami,
T.Tahara,
T.Kato,
H.Miyazaki,
and
R.Kuroki
(2004).
Structure of the receptor-binding domain of human thrombopoietin determined by complexation with a neutralizing antibody fragment.
|
| |
Proc Natl Acad Sci U S A,
101,
1816-1821.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
N.H.Carbonetti,
G.V.Artamonova,
C.Andreasen,
E.Dudley,
R.M.Mays,
and
Z.E.Worthington
(2004).
Suppression of serum antibody responses by pertussis toxin after respiratory tract colonization by Bordetella pertussis and identification of an immunodominant lipoprotein.
|
| |
Infect Immun,
72,
3350-3358.
|
|
|
|
|
|
|
R.F.Collins,
S.A.Frye,
A.Kitmitto,
R.C.Ford,
T.Tønjum,
and
J.P.Derrick
(2004).
Structure of the Neisseria meningitidis outer membrane PilQ secretin complex at 12 A resolution.
|
| |
J Biol Chem,
279,
39750-39756.
|
|
|
|
|
|
|
C.Bourgeois,
I.Okazaki,
E.Cavanaugh,
M.Nightingale,
and
J.Moss
(2003).
Identification of regulatory domains in ADP-ribosyltransferase-1 that determine transferase and NAD glycohydrolase activities.
|
| |
J Biol Chem,
278,
26351-26355.
|
|
|
|
|
|
|
E.Cascales,
and
P.J.Christie
(2003).
The versatile bacterial type IV secretion systems.
|
| |
Nat Rev Microbiol,
1,
137-149.
|
|
|
|
|
|
|
N.H.Carbonetti,
G.V.Artamonova,
R.M.Mays,
and
Z.E.Worthington
(2003).
Pertussis toxin plays an early role in respiratory tract colonization by Bordetella pertussis.
|
| |
Infect Immun,
71,
6358-6366.
|
|
|
|
|
|
|
T.H.Stenson,
A.K.Patton,
and
A.A.Weiss
(2003).
Reduced glutathione is required for pertussis toxin secretion by Bordetella pertussis.
|
| |
Infect Immun,
71,
1316-1320.
|
|
|
|
|
|
|
C.Wilde,
I.Just,
and
K.Aktories
(2002).
Structure-function analysis of the Rho-ADP-ribosylating exoenzyme C3stau2 from Staphylococcus aureus.
|
| |
Biochemistry,
41,
1539-1544.
|
|
|
|
|
|
|
K.M.Farizo,
S.Fiddner,
A.M.Cheung,
and
D.L.Burns
(2002).
Membrane localization of the S1 subunit of pertussis toxin in Bordetella pertussis and implications for pertussis toxin secretion.
|
| |
Infect Immun,
70,
1193-1201.
|
|
|
|
|
|
|
T.H.Stenson,
and
A.A.Weiss
(2002).
DsbA and DsbC are required for secretion of pertussis toxin by Bordetella pertussis.
|
| |
Infect Immun,
70,
2297-2303.
|
|
|
|
|
|
|
C.L.Drum,
Y.Shen,
P.A.Rice,
A.Bohm,
and
W.J.Tang
(2001).
Crystallization and preliminary X-ray study of the edema factor exotoxin adenylyl cyclase domain from Bacillus anthracis in the presence of its activator, calmodulin.
|
| |
Acta Crystallogr D Biol Crystallogr,
57,
1881-1884.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
M.J.Pallen,
A.C.Lam,
N.J.Loman,
and
A.McBride
(2001).
An abundance of bacterial ADP-ribosyltransferases--implications for the origin of exotoxins and their human homologues.
|
| |
Trends Microbiol,
9,
302.
|
|
|
|
|
|
|
N.H.Carbonetti,
R.G.Tuskan,
and
G.K.Lewis
(2001).
Stimulation of HIV gp120-specific cytolytic T lymphocyte responses in vitro and in vivo using a detoxified pertussis toxin vector.
|
| |
AIDS Res Hum Retroviruses,
17,
819-827.
|
|
|
|
|
|
|
R.Latif,
N.Kerlero de Rosbo,
T.Amarant,
R.Rappuoli,
G.Sappler,
and
A.Ben-Nun
(2001).
Reversal of the CD4(+)/CD8(+) T-cell ratio in lymph node cells upon in vitro mitogenic stimulation by highly purified, water-soluble S3-S4 dimer of pertussis toxin.
|
| |
Infect Immun,
69,
3073-3081.
|
|
|
|
|
|
|
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.
|
|
|
|
|
|
|
H.Otto,
D.Tezcan-Merdol,
R.Girisch,
F.Haag,
M.Rhen,
and
F.Koch-Nolte
(2000).
The spvB gene-product of the Salmonella enterica virulence plasmid is a mono(ADP-ribosyl)transferase.
|
| |
Mol Microbiol,
37,
1106-1115.
|
|
|
|
|
|
|
I.P.Nascimento,
W.O.Dias,
R.P.Mazzantini,
E.N.Miyaji,
M.Gamberini,
W.Quintilio,
V.C.Gebara,
D.F.Cardoso,
P.L.Ho,
I.Raw,
N.Winter,
B.Gicquel,
R.Rappuoli,
and
L.C.Leite
(2000).
Recombinant Mycobacterium bovis BCG expressing pertussis toxin subunit S1 induces protection against an intracerebral challenge with live Bordetella pertussis in mice.
|
| |
Infect Immun,
68,
4877-4883.
|
|
|
|
|
|
|
K.A.Craig-Mylius,
and
A.A.Weiss
(2000).
Antibacterial agents and release of periplasmic pertussis toxin from Bordetella pertussis.
|
| |
Antimicrob Agents Chemother,
44,
1383-1386.
|
|
|
|
|
|
|
K.A.Craig-Mylius,
T.H.Stenson,
and
A.A.Weiss
(2000).
Mutations in the S1 subunit of pertussis toxin that affect secretion.
|
| |
Infect Immun,
68,
1276-1281.
|
|
|
|
|
|
|
K.M.Farizo,
T.Huang,
and
D.L.Burns
(2000).
Importance of holotoxin assembly in Ptl-mediated secretion of pertussis toxin from Bordetella pertussis.
|
| |
Infect Immun,
68,
4049-4054.
|
|
|
|
|
|
|
S.Z.Hausman,
and
D.L.Burns
(2000).
Use of pertussis toxin encoded by ptx genes from Bordetella bronchiseptica to model the effects of antigenic drift of pertussis toxin on antibody neutralization.
|
| |
Infect Immun,
68,
3763-3767.
|
|
|
|
|
|
|
Y.Momoi,
K.Ichiyama,
I.H.Chowdhury,
Y.Koyanagi,
and
N.Yamamoto
(2000).
Pertussis toxin enhances human immunodeficiency virus type 1 replication.
|
| |
AIDS Res Hum Retroviruses,
16,
373-379.
|
|
|
|
|
|
|
D.L.Burns
(1999).
Biochemistry of type IV secretion.
|
| |
Curr Opin Microbiol,
2,
25-29.
|
|
|
|
|
|
|
D.R.Hall,
D.G.Gourley,
G.A.Leonard,
E.M.Duke,
L.A.Anderson,
D.H.Boxer,
and
W.N.Hunter
(1999).
The high-resolution crystal structure of the molybdate-dependent transcriptional regulator (ModE) from Escherichia coli: a novel combination of domain folds.
|
| |
EMBO J,
18,
1435-1446.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
G.Spraggon
(1999).
Envelope skeletonization as a means to determine monomer masks and non-crystallographic symmetry relationships: application in the solution of the structure of fibrinogen fragment D.
|
| |
Acta Crystallogr D Biol Crystallogr,
55,
458-463.
|
|
|
|
|
|
|
K.A.Craig-Mylius,
and
A.A.Weiss
(1999).
Mutants in the ptlA-H genes of Bordetella pertussis are deficient for pertussis toxin secretion.
|
| |
FEMS Microbiol Lett,
179,
479-484.
|
|
|
|
|
|
|
N.H.Carbonetti,
T.J.Irish,
C.H.Chen,
C.B.O'Connell,
G.A.Hadley,
U.McNamara,
R.G.Tuskan,
and
G.K.Lewis
(1999).
Intracellular delivery of a cytolytic T-lymphocyte epitope peptide by pertussis toxin to major histocompatibility complex class I without involvement of the cytosolic class I antigen processing pathway.
|
| |
Infect Immun,
67,
602-607.
|
|
|
|
|
|
|
N.Nagano,
E.G.Hutchinson,
and
J.M.Thornton
(1999).
Barrel structures in proteins: automatic identification and classification including a sequence analysis of TIM barrels.
|
| |
Protein Sci,
8,
2072-2084.
|
|
|
|
|
|
|
A.Nandi,
K.Suguna,
A.Surolia,
and
S.S.Visweswariah
(1998).
Topological mimicry and epitope duplication in the guanylyl cyclase C receptor.
|
| |
Protein Sci,
7,
2175-2183.
|
|
|
|
|
|
|
A.Ruf,
G.de Murcia,
and
G.E.Schulz
(1998).
Inhibitor and NAD+ binding to poly(ADP-ribose) polymerase as derived from crystal structures and homology modeling.
|
| |
Biochemistry,
37,
3893-3900.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
D.B.Lacy,
and
R.C.Stevens
(1998).
Unraveling the structures and modes of action of bacterial toxins.
|
| |
Curr Opin Struct Biol,
8,
778-784.
|
|
|
|
|
|
|
G.Del Giudice,
M.Pizza,
and
R.Rappuoli
(1998).
Molecular basis of vaccination.
|
| |
Mol Aspects Med,
19,
1.
|
|
|
|
|
|
|
H.Barth,
J.C.Preiss,
F.Hofmann,
and
K.Aktories
(1998).
Characterization of the catalytic site of the ADP-ribosyltransferase Clostridium botulinum C2 toxin by site-directed mutagenesis.
|
| |
J Biol Chem,
273,
29506-29511.
|
|
|
|
|
|
|
J.Scheuring,
P.J.Berti,
and
V.L.Schramm
(1998).
Transition-state structure for the ADP-ribosylation of recombinant Gialpha1 subunits by pertussis toxin.
|
| |
Biochemistry,
37,
2748-2758.
|
|
|
|
|
|
|
M.Degano,
S.C.Almo,
J.C.Sacchettini,
and
V.L.Schramm
(1998).
Trypanosomal nucleoside hydrolase. A novel mechanism from the structure with a transition-state inhibitor.
|
| |
Biochemistry,
37,
6277-6285.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
A.Suarez,
L.H.Staendner,
M.Rohde,
G.Piatti,
K.N.Timmis,
and
C.A.Guzmán
(1997).
Stable expression of pertussis toxin in Bordetella bronchiseptica under the control of a tightly regulated promoter.
|
| |
Appl Environ Microbiol,
63,
122-127.
|
|
|
|
|
|
|
B.B.Finlay,
and
S.Falkow
(1997).
Common themes in microbial pathogenicity revisited.
|
| |
Microbiol Mol Biol Rev,
61,
136-169.
|
|
|
|
|
|
|
B.Hazes,
and
R.J.Read
(1997).
Accumulating evidence suggests that several AB-toxins subvert the endoplasmic reticulum-associated protein degradation pathway to enter target cells.
|
| |
Biochemistry,
36,
11051-11054.
|
|
|
|
|
|
|
C.E.Bell,
and
D.Eisenberg
(1997).
Crystal structure of nucleotide-free diphtheria toxin.
|
| |
Biochemistry,
36,
481-488.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
G.S.Prasad,
R.Radhakrishnan,
D.T.Mitchell,
C.A.Earhart,
M.M.Dinges,
W.J.Cook,
P.M.Schlievert,
and
D.H.Ohlendorf
(1997).
Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activity.
|
| |
Protein Sci,
6,
1220-1227.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
J.Rossjohn,
J.T.Buckley,
B.Hazes,
A.G.Murzin,
R.J.Read,
and
M.W.Parker
(1997).
Aerolysin and pertussis toxin share a common receptor-binding domain.
|
| |
EMBO J,
16,
3426-3434.
|
|
|
|
|
|
|
M.Bycroft,
T.J.Hubbard,
M.Proctor,
S.M.Freund,
and
A.G.Murzin
(1997).
The solution structure of the S1 RNA binding domain: a member of an ancient nucleic acid-binding fold.
|
| |
Cell,
88,
235-242.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
V.Rolli,
M.O'Farrell,
J.Ménissier-de Murcia,
and
G.de Murcia
(1997).
Random mutagenesis of the poly(ADP-ribose) polymerase catalytic domain reveals amino acids involved in polymer branching.
|
| |
Biochemistry,
36,
12147-12154.
|
|
|
|
|
|
|
A.Ruf,
J.Mennissier de Murcia,
G.de Murcia,
and
G.E.Schulz
(1996).
Structure of the catalytic fragment of poly(AD-ribose) polymerase from chicken.
|
| |
Proc Natl Acad Sci U S A,
93,
7481-7485.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
C.E.Bell,
and
D.Eisenberg
(1996).
Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide.
|
| |
Biochemistry,
35,
1137-1149.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
D.Kohda,
C.J.Morton,
A.A.Parkar,
H.Hatanaka,
F.M.Inagaki,
I.D.Campbell,
and
A.J.Day
(1996).
Solution structure of the link module: a hyaluronan-binding domain involved in extracellular matrix stability and cell migration.
|
| |
Cell,
86,
767-775.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
F.van den Akker,
S.Sarfaty,
E.M.Twiddy,
T.D.Connell,
R.K.Holmes,
and
W.G.Hol
(1996).
Crystal structure of a new heat-labile enterotoxin, LT-IIb.
|
| |
Structure,
4,
665-678.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
M.Li,
F.Dyda,
I.Benhar,
I.Pastan,
and
D.R.Davies
(1996).
Crystal structure of the catalytic domain of Pseudomonas exotoxin A complexed with a nicotinamide adenine dinucleotide analog: implications for the activation process and for ADP ribosylation.
|
| |
Proc Natl Acad Sci U S A,
93,
6902-6906.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
P.Kaul,
J.Silverman,
W.H.Shen,
S.R.Blanke,
P.D.Huynh,
A.Finkelstein,
and
R.J.Collier
(1996).
Roles of Glu 349 and Asp 352 in membrane insertion and translocation by diphtheria toxin.
|
| |
Protein Sci,
5,
687-692.
|
|
|
|
|
|
|
S.Z.Hausman,
J.D.Cherry,
U.Heininger,
C.H.Wirsing von König,
and
D.L.Burns
(1996).
Analysis of proteins encoded by the ptx and ptl genes of Bordetella bronchiseptica and Bordetella parapertussis.
|
| |
Infect Immun,
64,
4020-4026.
|
|
|
|
|
|
|
V.Finck-Barbançon,
and
J.T.Barbieri
(1996).
Preferential processing of the S1 subunit of pertussis toxin that is bound to eukaryotic cells.
|
| |
Mol Microbiol,
22,
87-95.
|
|
|
|
|
|
|
E.A.Merritt,
and
W.G.Hol
(1995).
AB5 toxins.
|
| |
Curr Opin Struct Biol,
5,
165-171.
|
|
|
|
|
|
|
G.T.Marsischky,
B.A.Wilson,
and
R.J.Collier
(1995).
Role of glutamic acid 988 of human poly-ADP-ribose polymerase in polymer formation. Evidence for active site similarities to the ADP-ribosylating toxins.
|
| |
J Biol Chem,
270,
3247-3254.
|
|
|
|
|
|
|
K.M.Krueger,
and
J.T.Barbieri
(1995).
The family of bacterial ADP-ribosylating exotoxins.
|
| |
Clin Microbiol Rev,
8,
34-47.
|
|
|
|
|
|
|
M.Li,
F.Dyda,
I.Benhar,
I.Pastan,
and
D.R.Davies
(1995).
The crystal structure of Pseudomonas aeruginosa exotoxin domain III with nicotinamide and AMP: conformational differences with the intact exotoxin.
|
| |
Proc Natl Acad Sci U S A,
92,
9308-9312.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
R.Manetti,
P.Massari,
D.Burroni,
M.de Bernard,
A.Marchini,
R.Olivieri,
E.Papini,
C.Montecucco,
R.Rappuoli,
and
J.L.Telford
(1995).
Helicobacter pylori cytotoxin: importance of native conformation for induction of neutralizing antibodies.
|
| |
Infect Immun,
63,
4476-4480.
|
|
|
|
|
|
|
R.Shahin,
M.Leef,
J.Eldridge,
M.Hudson,
and
R.Gilley
(1995).
Adjuvanticity and protective immunity elicited by Bordetella pertussis antigens encapsulated in poly(DL-lactide-co-glycolide) microspheres.
|
| |
Infect Immun,
63,
1195-1200.
|
|
|
|
|
|
|
T.Takada,
K.Iida,
and
J.Moss
(1995).
Conservation of a common motif in enzymes catalyzing ADP-ribose transfer. Identification of domains in mammalian transferases.
|
| |
J Biol Chem,
270,
541-544.
|
|
|
|
|
|
|
Y.Xu,
and
J.T.Barbieri
(1995).
Pertussis toxin-mediated ADP-ribosylation of target proteins in Chinese hamster ovary cells involves a vesicle trafficking mechanism.
|
| |
Infect Immun,
63,
825-832.
|
|
|
|
|
|
|
Z.Shao,
and
J.Yang
(1995).
Progress in high resolution atomic force microscopy in biology.
|
| |
Q Rev Biophys,
28,
195-251.
|
|
|
|
|
|
|
F.Lynn,
W.N.Burnette,
G.R.Siber,
and
J.L.Arciniega
(1994).
Human antibody response to the B oligomer of pertussis toxin.
|
| |
Clin Diagn Lab Immunol,
1,
626-632.
|
|
|
|
|
|
|
G.D.Armstrong,
C.G.Clark,
and
L.D.Heerze
(1994).
The 70-kilodalton pertussis toxin-binding protein in Jurkat cells.
|
| |
Infect Immun,
62,
2236-2243.
|
|
|
|
|
|
|
G.Menestrina,
G.Schiavo,
and
C.Montecucco
(1994).
Molecular mechanisms of action of bacterial protein toxins.
|
| |
Mol Aspects Med,
15,
79.
|
|
|
|
|
|
|
J.Janin
(1994).
Proteins with a ring.
|
| |
Structure,
2,
571-573.
|
|
|
|
|
|
|
J.Sandros,
E.Rozdzinski,
J.Zheng,
D.Cowburn,
and
E.Tuomanen
(1994).
Lectin domains in the toxin of Bordetella pertussis: selectin mimicry linked to microbial pathogenesis.
|
| |
Glycoconj J,
11,
501-506.
|
|
|
|
|
|
|
K.M.Krueger,
and
J.T.Barbieri
(1994).
Assignment of functional domains involved in ADP-ribosylation and B-oligomer binding within the carboxyl terminus of the S1 subunit of pertussis toxin.
|
| |
Infect Immun,
62,
2071-2078.
|
|
|
|
|
|
|
L.Holm,
and
C.Sander
(1994).
Searching protein structure databases has come of age.
|
| |
Proteins,
19,
165-173.
|
|
|
|
|
|
|
M.Domenighini,
C.Magagnoli,
M.Pizza,
and
R.Rappuoli
(1994).
Common features of the NAD-binding and catalytic site of ADP-ribosylating toxins.
|
| |
Mol Microbiol,
14,
41-50.
|
|
|
|
|
|
|
M.J.Bennett,
S.Choe,
and
D.Eisenberg
(1994).
Refined structure of dimeric diphtheria toxin at 2.0 A resolution.
|
| |
Protein Sci,
3,
1444-1463.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
P.E.Stein,
A.Boodhoo,
G.D.Armstrong,
L.D.Heerze,
S.A.Cockle,
M.H.Klein,
and
R.J.Read
(1994).
Structure of a pertussis toxin-sugar complex as a model for receptor binding.
|
| |
Nat Struct Biol,
1,
591-596.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
W.N.Burnette
(1994).
AB5 ADP-ribosylating toxins: comparative anatomy and physiology.
|
| |
Structure,
2,
151-158.
|
|
|
|
|
|
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.
|
| |
Links
