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Oxidoreductase
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PDB id
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1nwa
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.1.8.4.11
- Peptide-methionine (S)-S-oxide reductase.
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Reaction:
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1.
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Peptide-L-methionine + thioredoxin disulfide + H2O = peptide-L- methionine (S)-S-oxide + thioredoxin
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2.
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L-methionine + thioredoxin disulfide + H2O = L-methionine (S)-S- oxide + thioredoxin
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Peptide-L-methionine
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+
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thioredoxin disulfide
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+
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H(2)O
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=
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peptide-L- methionine (S)-S-oxide
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+
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thioredoxin
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L-methionine
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+
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thioredoxin disulfide
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+
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H(2)O
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=
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L-methionine (S)-S- oxide
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+
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thioredoxin
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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Gene Ontology (GO) functional annotation
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Biological process
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oxidation reduction
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4 terms
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Biochemical function
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oxidoreductase activity
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4 terms
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DOI no:
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J Bacteriol
185:4119-4126
(2003)
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PubMed id:
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Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
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A.B.Taylor,
D.M.Benglis,
S.Dhandayuthapani,
P.J.Hart.
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ABSTRACT
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Peptide methionine sulfoxide reductase (MsrA) repairs oxidative damage to
methionine residues arising from reactive oxygen species and reactive nitrogen
intermediates. MsrA activity is found in a wide variety of organisms, and it is
implicated as one of the primary defenses against oxidative stress. Disruption
of the gene encoding MsrA in several pathogenic bacteria responsible for
infections in humans results in the loss of their ability to colonize host
cells. Here, we present the X-ray crystal structure of MsrA from the pathogenic
bacterium Mycobacterium tuberculosis refined to 1.5 A resolution. In contrast to
the three catalytic cysteine residues found in previously characterized MsrA
structures, M. tuberculosis MsrA represents a class containing only two
functional cysteine residues. The structure reveals a methionine residue of one
MsrA molecule bound at the active site of a neighboring molecule in the crystal
lattice and thus serves as an excellent model for protein-bound methionine
sulfoxide recognition and repair.
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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.G.Arias,
M.S.Cabeza,
E.D.Erben,
P.G.Carranza,
H.D.Lujan,
M.T.Téllez Iñón,
A.A.Iglesias,
and
S.A.Guerrero
(2011).
Functional characterization of methionine sulfoxide reductase A from Trypanosoma spp.
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Free Radic Biol Med, 50,
37-46.
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D.T.Le,
B.C.Lee,
S.M.Marino,
Y.Zhang,
D.E.Fomenko,
A.Kaya,
E.Hacioglu,
G.H.Kwak,
A.Koc,
H.Y.Kim,
and
V.N.Gladyshev
(2009).
Functional analysis of free methionine-R-sulfoxide reductase from Saccharomyces cerevisiae.
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J Biol Chem, 284,
4354-4364.
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S.A.Stalford,
M.A.Fascione,
S.J.Sasindran,
D.Chatterjee,
S.Dhandayuthapani,
and
W.B.Turnbull
(2009).
A natural carbohydrate substrate for Mycobacterium tuberculosis methionine sulfoxide reductase A.
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Chem Commun (Camb), 0,
110-112.
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Y.K.Kim,
Y.J.Shin,
W.H.Lee,
H.Y.Kim,
and
K.Y.Hwang
(2009).
Structural and kinetic analysis of an MsrA-MsrB fusion protein from Streptococcus pneumoniae.
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Mol Microbiol, 72,
699-709.
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PDB codes:
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L.Shi,
C.D.Sohaskey,
R.J.North,
and
M.L.Gennaro
(2008).
Transcriptional characterization of the antioxidant response of Mycobacterium tuberculosis in vivo and during adaptation to hypoxia in vitro.
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Tuberculosis (Edinb), 88,
1-6.
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S.J.Sasindran,
S.Saikolappan,
and
S.Dhandayuthapani
(2007).
Methionine sulfoxide reductases and virulence of bacterial pathogens.
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Future Microbiol, 2,
619-630.
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H.Y.Kim,
D.E.Fomenko,
Y.E.Yoon,
and
V.N.Gladyshev
(2006).
Catalytic advantages provided by selenocysteine in methionine-S-sulfoxide reductases.
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Biochemistry, 45,
13697-13704.
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A.Olry,
S.Boschi-Muller,
H.Yu,
D.Burnel,
and
G.Branlant
(2005).
Insights into the role of the metal binding site in methionine-R-sulfoxide reductases B.
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Protein Sci, 14,
2828-2837.
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H.Y.Kim,
and
V.N.Gladyshev
(2005).
Different catalytic mechanisms in mammalian selenocysteine- and cysteine-containing methionine-R-sulfoxide reductases.
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PLoS Biol, 3,
e375.
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M.F.Hiltz,
G.R.Sisson,
A.K.Brassinga,
E.Garduno,
R.A.Garduno,
and
P.S.Hoffman
(2004).
Expression of magA in Legionella pneumophila Philadelphia-1 is developmentally regulated and a marker of formation of mature intracellular forms.
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J Bacteriol, 186,
3038-3045.
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N.Coudevylle,
A.Thureau,
S.Azza,
S.Boshi-Muller,
G.Branlant,
and
M.T.Cung
(2004).
(1)H, (13)C and (15)N resonance assignment of the reduced form of methionine sulfoxide reductase A from Escherichia coli.
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J Biomol NMR, 30,
363-364.
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C.V.Smith,
and
J.C.Sacchettini
(2003).
Mycobacterium tuberculosis: a model system for structural genomics.
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| |
Curr Opin Struct Biol, 13,
658-664.
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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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Links
