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PDBsum entry 1ts3
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Contents |
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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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H135a mutant of toxic shock syndrome toxin-1 from s. Aureus
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Structure:
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Toxic shock syndrome toxin-1. Chain: a, b, c. Synonym: tsst-1. Engineered: yes. Mutation: yes
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Source:
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Staphylococcus aureus. Organism_taxid: 1280. Expressed in: staphylococcus aureus. Expression_system_taxid: 1280
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Biol. unit:
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Monomer (from PDB file)
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Resolution:
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2.00Å
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R-factor:
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not given
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Authors:
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C.A.Earhart,D.T.Mitchell,D.L.Murray,D.M.Pinheiro,M.Matsumura, P.M.Schlievert,D.H.Ohlendorf
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Key ref:
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C.A.Earhart
et al.
(1998).
Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.
Biochemistry,
37,
7194-7202.
PubMed id:
DOI:
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Date:
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10-Oct-97
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Release date:
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16-Dec-98
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PROCHECK
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Headers
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References
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P06886
(TSST_STAAU) -
Toxic shock syndrome toxin-1 from Staphylococcus aureus
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Seq:
Struc:
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234 a.a.
194 a.a.*
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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*
PDB and UniProt seqs differ
at 2 residue positions (black
crosses)
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DOI no:
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Biochemistry
37:7194-7202
(1998)
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PubMed id:
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Structures of five mutants of toxic shock syndrome toxin-1 with reduced biological activity.
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C.A.Earhart,
D.T.Mitchell,
D.L.Murray,
D.M.Pinheiro,
M.Matsumura,
P.M.Schlievert,
D.H.Ohlendorf.
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ABSTRACT
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The three-dimensional structures of five mutants of toxic shock syndrome toxin-1
(TSST-1) have been determined. These mutations are in the long central alpha
helix and are useful in mapping portions of TSST-1 involved in superantigenicity
and lethality. The T128A, H135A, Q139K, and I140T mutations appear to reduce
superantigenicity by altering the properties of the T-cell receptor interaction
surface. The Q136A mutation is at a largely buried site and causes a dramatic
change in the conformation of the beta7-beta9 loop which covers the back of the
central alpha helix. As this mutation has the unique ability to reduce the
toxin's lethality in rabbits while retaining its superantigenicity, it raises
the possibility that this rear loop mediates the ability of TSST-1 to induce
lethality and suggests a route for producing nonlethal toxins for therapeutic
development.
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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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A.J.Brosnahan,
M.M.Schaefers,
W.H.Amundson,
M.J.Mantz,
C.A.Squier,
M.L.Peterson,
and
P.M.Schlievert
(2008).
Novel toxic shock syndrome toxin-1 amino acids required for biological activity.
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Biochemistry,
47,
12995-13003.
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D.Devore-Carter,
S.Kar,
V.Vellucci,
V.Bhattacherjee,
P.Domanski,
and
M.K.Hostetter
(2008).
Superantigen-like effects of a Candida albicans polypeptide.
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J Infect Dis,
197,
981-989.
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Y.Kuwahara,
A.Ohno,
T.Morii,
H.Yokoyama,
I.Matsui,
H.Tochio,
M.Shirakawa,
and
H.Hiroaki
(2008).
The solution structure of the C-terminal domain of NfeD reveals a novel membrane-anchored OB-fold.
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Protein Sci,
17,
1915-1924.
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PDB code:
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A.Zemla,
B.Geisbrecht,
J.Smith,
M.Lam,
B.Kirkpatrick,
M.Wagner,
T.Slezak,
and
C.E.Zhou
(2007).
STRALCP--structure alignment-based clustering of proteins.
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Nucleic Acids Res,
35,
e150.
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A.Bavoso,
A.Ostuni,
J.De Vendel,
F.Pollaro,
F.Armentano,
T.Knight,
S.Makker,
and
A.Tramontano
(2006).
Aldehyde modification of peptide immunogen enhances protein-reactive antibody response to toxic shock syndrome toxin-1.
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J Pept Sci,
12,
843-849.
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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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J.K.McCormick,
J.M.Yarwood,
and
P.M.Schlievert
(2001).
Toxic shock syndrome and bacterial superantigens: an update.
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Annu Rev Microbiol,
55,
77.
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M.M.Dinges,
P.M.Orwin,
and
P.M.Schlievert
(2000).
Exotoxins of Staphylococcus aureus.
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Clin Microbiol Rev,
13,
16.
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W.W.Kum,
K.B.Laupland,
and
A.W.Chow
(2000).
Defining a novel domain of staphylococcal toxic shock syndrome toxin-1 critical for major histocompatibility complex class II binding, superantigenic activity, and lethality.
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Can J Microbiol,
46,
171-179.
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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
