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PDBsum entry 3seb
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* Residue conservation analysis
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DOI no:
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J Mol Biol
277:61-79
(1998)
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PubMed id:
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Crystal structure of microbial superantigen staphylococcal enterotoxin B at 1.5 A resolution: implications for superantigen recognition by MHC class II molecules and T-cell receptors.
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A.C.Papageorgiou,
H.S.Tranter,
K.R.Acharya.
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ABSTRACT
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Staphylococcal enterotoxin B is a member of a family of toxins known as
superantigens that activate a large number of T-cells (up to 20%) by
cross-linking MHC class II molecules with T-cell receptors in a Vbeta-restricted
fashion. The crystal structure of staphylococcal enterotoxin B presented here
has been determined at 1.5 A resolution, the highest resolution so far for a
superantigen. The final model contains 1948 protein atoms and 177 water
molecules and has excellent geometry with root-mean-square (rms) deviation of
0.007 A and 1.73 degrees in bond lengths and bond angles, respectively. The
overall fold is similar to that of other microbial superantigens, but as it
lacks the zinc-binding site found in other members of this family, such as
staphylococcal enterotoxin A, C2 and D, this enterotoxin possesses only one MHC
class II binding site. Comparison of the crystal structure of free SEB and in
complex with an MHC class II molecule revealed no major changes in the
MHC-binding site upon complex formation. However, a number of water molecules
found in the free SEB may be displaced in the complex or contribute further to
its stability. Detailed analysis of the TcR-binding site of SEB, SEA and SEC2
shows significant differences which may account for the ability of each
superantigen to bind specific Vbeta sequences.
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Selected figure(s)
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Figure 6.
Figure 6. Stereo views displaying (a) a C^α-trace of SEB
(every tenth residue is numbered); and (b) a comparison of
C^α-traces of SEB (black), SEC2 (green), SEA (blue) and TSST-1
(orange).
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Figure 9.
Figure 9. Histogram of the B-factor distribution for the
water molecules in SEB.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(1998,
277,
61-79)
copyright 1998.
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Figures were
selected
by an automated process.
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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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S.Yanaka,
M.Kudou,
Y.Tanaka,
T.Sasaki,
S.Takemoto,
A.Sakata,
Y.Hattori,
T.Koshi,
S.Futaki,
K.Tsumoto,
and
T.Nakashima
(2010).
Contribution of the flexible loop region to the function of staphylococcal enterotoxin B.
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Protein Eng Des Sel,
23,
415-421.
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PDB code:
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T.K.Inskeep,
C.Stahl,
J.Odle,
J.Oakes,
L.Hudson,
K.L.Bost,
and
K.J.Piller
(2010).
Oral vaccine formulations stimulate mucosal and systemic antibody responses against staphylococcal enterotoxin B in a piglet model.
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Clin Vaccine Immunol,
17,
1163-1169.
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J.Hui,
Y.Cao,
F.Xiao,
J.Zhang,
H.Li,
and
F.Hu
(2008).
Staphylococcus aureus enterotoxin C2 mutants: biological activity assay in vitro.
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J Ind Microbiol Biotechnol,
35,
975-980.
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Z.G.Chen
(2008).
Conductometric immunosensors for the detection of staphylococcal enterotoxin B based bio-electrocalytic reaction on micro-comb electrodes.
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Bioprocess Biosyst Eng,
31,
345-350.
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A.M.Burroughs,
S.Balaji,
L.M.Iyer,
and
L.Aravind
(2007).
Small but versatile: the extraordinary functional and structural diversity of the beta-grasp fold.
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Biol Direct,
2,
18.
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K.Yamada,
I.Sanzen,
T.Ohkura,
A.Okamoto,
K.Torii,
T.Hasegawa,
and
M.Ohta
(2007).
Analysis of twin-arginine translocation pathway homologue in Staphylococcus aureus.
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Curr Microbiol,
55,
14-19.
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M.M.Fernández,
S.Bhattacharya,
M.C.De Marzi,
P.H.Brown,
M.Kerzic,
P.Schuck,
R.A.Mariuzza,
and
E.L.Malchiodi
(2007).
Superantigen natural affinity maturation revealed by the crystal structure of staphylococcal enterotoxin G and its binding to T-cell receptor Vbeta8.2.
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Proteins,
68,
389-402.
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B.V.Geisbrecht,
B.Y.Hamaoka,
B.Perman,
A.Zemla,
and
D.J.Leahy
(2005).
The crystal structures of EAP domains from Staphylococcus aureus reveal an unexpected homology to bacterial superantigens.
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J Biol Chem,
280,
17243-17250.
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PDB codes:
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G.Wang,
and
R.G.Carbonell
(2005).
Characterization of a peptide affinity support that binds selectively to staphylococcal enterotoxin B.
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J Chromatogr A,
1078,
98.
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M.Möllhoff,
H.B.Zanden,
P.R.Shiflett,
and
G.Gupta
(2005).
Modeling of receptor mimics that inhibit superantigen pathogenesis.
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J Mol Recognit,
18,
73-83.
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A.C.Papageorgiou,
M.D.Baker,
J.D.McLeod,
S.K.Goda,
C.N.Manzotti,
D.M.Sansom,
H.S.Tranter,
and
K.R.Acharya
(2004).
Identification of a secondary zinc-binding site in staphylococcal enterotoxin C2. Implications for superantigen recognition.
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J Biol Chem,
279,
1297-1303.
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PDB codes:
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E.Hong-Geller,
M.Möllhoff,
P.R.Shiflett,
and
G.Gupta
(2004).
Design of chimeric receptor mimics with different TcRVbeta isoforms. Type-specific inhibition of superantigen pathogenesis.
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J Biol Chem,
279,
5676-5684.
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T.J.Tripp,
J.K.McCormick,
J.M.Webb,
and
P.M.Schlievert
(2003).
The zinc-dependent major histocompatibility complex class II binding site of streptococcal pyrogenic exotoxin C is critical for maximal superantigen function and toxic activity.
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Infect Immun,
71,
1548-1550.
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W.G.Purschke,
F.Radtke,
F.Kleinjung,
and
S.Klussmann
(2003).
A DNA Spiegelmer to staphylococcal enterotoxin B.
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Nucleic Acids Res,
31,
3027-3032.
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H.Pettersson,
and
G.Forsberg
(2002).
Staphylococcal enterotoxin H contrasts closely related enterotoxins in species reactivity.
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Immunology,
106,
71-79.
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J.W.Shupp,
M.Jett,
and
C.H.Pontzer
(2002).
Identification of a transcytosis epitope on staphylococcal enterotoxins.
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Infect Immun,
70,
2178-2186.
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Y.I.Chi,
I.Sadler,
L.M.Jablonski,
S.D.Callantine,
C.F.Deobald,
C.V.Stauffacher,
and
G.A.Bohach
(2002).
Zinc-mediated dimerization and its effect on activity and conformation of staphylococcal enterotoxin type C.
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J Biol Chem,
277,
22839-22846.
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PDB code:
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A.C.Papageorgiou,
and
K.R.Acharya
(2000).
Microbial superantigens: from structure to function.
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Trends Microbiol,
8,
369-375.
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H.R.Churchill,
P.S.Andersen,
E.A.Parke,
R.A.Mariuzza,
and
D.M.Kranz
(2000).
Mapping the energy of superantigen Staphylococcus enterotoxin C3 recognition of an alpha/beta T cell receptor using alanine scanning mutagenesis.
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J Exp Med,
191,
835-846.
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L.T.Pang,
W.W.Kum,
and
A.W.Chow
(2000).
Inhibition of staphylococcal enterotoxin B-induced lymphocyte proliferation and tumor necrosis factor alpha secretion by MAb5, an anti-toxic shock syndrome toxin 1 monoclonal antibody.
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Infect Immun,
68,
3261-3268.
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M.Graille,
E.A.Stura,
A.L.Corper,
B.J.Sutton,
M.J.Taussig,
J.B.Charbonnier,
and
G.J.Silverman
(2000).
Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity.
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Proc Natl Acad Sci U S A,
97,
5399-5404.
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PDB code:
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A.C.Papageorgiou,
C.M.Collins,
D.M.Gutman,
J.B.Kline,
S.M.O'Brien,
H.S.Tranter,
and
K.R.Acharya
(1999).
Structural basis for the recognition of superantigen streptococcal pyrogenic exotoxin A (SpeA1) by MHC class II molecules and T-cell receptors.
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EMBO J,
18,
9.
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PDB code:
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P.M.Lavoie,
J.Thibodeau,
F.Erard,
and
R.P.Sékaly
(1999).
Understanding the mechanism of action of bacterial superantigens from a decade of research.
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Immunol Rev,
168,
257-269.
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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
code is
shown on the right.
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Links
