DB code: S00277

CATH domain 3.30.1060.10 : Peptide Methionine Sulfoxide Reductase; Chain A Catalytic domain
E.C. 1.8.4.11
CSA 1fva 1ff3
M-CSA 1fva 1ff3
MACiE M0122

CATH domain Related DB codes (homologues)
3.30.1060.10 : Peptide Methionine Sulfoxide Reductase; Chain A S00523

Uniprot Enzyme Name
UniprotKB Protein name Synonyms RefSeq Pfam
P0A744 Peptide methionine sulfoxide reductase MsrA
Protein-methionine-S-oxide reductase
EC 1.8.4.11
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase
NP_418640.1 (Protein)
NC_000913.2 (DNA/RNA sequence)
YP_492361.1 (Protein)
NC_007779.1 (DNA/RNA sequence)
PF01625 (PMSR)
[Graphical View]
P54149 Mitochondrial peptide methionine sulfoxide reductase
EC 1.8.4.11
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase
Protein-methionine-S-oxide reductase
NP_776539.1 (Protein)
NM_174114.2 (DNA/RNA sequence)
PF01625 (PMSR)
[Graphical View]

KEGG enzyme name
peptide-methionine (S)-S-oxide reductase
MsrA
methionine sulfoxide reductase (ambiguous)
methionine sulphoxide reductase A
methionine S-oxide reductase (ambiguous)
methionine S-oxide reductase (S-form oxidizing)
methionine sulfoxide reductase A
peptide methionine sulfoxide reductase

UniprotKB: Accession Number Entry name Activity Subunit Subcellular location Cofactor
P54149 MSRA_BOVIN Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.
P0A744 MSRA_ECOLI Peptide-L-methionine + thioredoxin disulfide + H(2)O = peptide-L-methionine (S)-S-oxide + thioredoxin. L-methionine + thioredoxin disulfide + H(2)O = L-methionine (S)-S-oxide + thioredoxin.

KEGG Pathways
Map code Pathways E.C.

Compound table
Substrates Products Intermediates
KEGG-id C03895 C00342 C15999 C03023 C00343 C00001 C00073
E.C.
Compound Peptide-L-methionine (S)-S-oxide Reduced thioredoxin L-methionine (S)-S-oxide Peptide-L-methionine Oxidized thioredoxin H2O L-methionine
Type peptide/protein,sulfoxide group amide group,carbohydrate,peptide/protein,sulfhydryl group amino acids,sulfoxide group peptide/protein,sulfide group amide group,carbohydrate,disulfide bond,peptide/protein H2O amino acids,sulfide group
ChEBI 49031
58772
15377
16643
57844
PubChem 10909908
11869257
22247451
962
6137
6992087
1ff3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ff3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1ff3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fvaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fvaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Unbound Unbound Unbound Unbound Unbound Unbound
1fvgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain Unbound Analogue:DTT Unbound Unbound Unbound Unbound Intermediate-analogue:DTT

Reference for Active-site residues
resource references E.C.
PDB;1fvg

Active-site residues
PDB Catalytic residues Cofactor-binding residues Modified residues Main-chain involved in catalysis Comment
1ff3A Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;TYR 82;GLU 94;TYR 134;CYS 198;CYS 206 CAS 51
1ff3B Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;TYR 82;GLU 94;TYR 134; ; CAS 51 invisible 195-211
1ff3C Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain ;TYR 82;GLU 94;TYR 134; ; CAS 51 invisible 193-211
1fvaA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 72;TYR 103;GLU 115;TYR 155;CYS 218;CYS 227
1fvaB Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 72;TYR 103;GLU 115;TYR 155;CYS 218;CYS 227
1fvgA Pdbj logo s Rasmollogo id Rasmollogo chain Mmcif id Mmcif chain CYS 72;TYR 103;GLU 115;TYR 155;CYS 218; truncation 219-228

References for Catalytic Mechanism
References Sections No. of steps in catalysis
[1]
Fig.3, p.13310-13311
[2]
Fig.1, p.35911-35913
[4]
Fig.3, p.6466-6467
[5]
Fig.8, p.1175-1176
[9]
Scheme 5, p.402-404
[15]
p.4121-4125

References
[1]
Resource
Comments X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
Medline ID 20519025
PubMed ID 11063566
Journal Biochemistry
Year 2000
Volume 39
Pages 13307-12
Authors Lowther WT, Brot N, Weissbach H, Matthews BW
Title Structure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme.
Related PDB 1fva 1fvg
Related UniProtKB P54149
[2]
Resource
Comments
Medline ID
PubMed ID 10964927
Journal J Biol Chem
Year 2000
Volume 275
Pages 35908-13
Authors Boschi-Muller S, Azza S, Sanglier-Cianferani S, Talfournier F, Van Dorsselear A, Branlant G
Title A sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.
Related PDB
Related UniProtKB
[3]
Resource
Comments
Medline ID
PubMed ID 10799493
Journal J Biol Chem
Year 2000
Volume 275
Pages 14167-72
Authors Moskovitz J, Poston JM, Berlett BS, Nosworthy NJ, Szczepanowski R, Stadtman ER
Title Identification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.
Related PDB
Related UniProtKB
[4]
Resource
Comments
Medline ID
PubMed ID 10841552
Journal Proc Natl Acad Sci U S A
Year 2000
Volume 97
Pages 6463-8
Authors Lowther WT, Brot N, Weissbach H, Honek JF, Matthews BW
Title Thiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase.
Related PDB
Related UniProtKB
[5]
Resource
Comments
Medline ID
PubMed ID 11080639
Journal Structure Fold Des
Year 2000
Volume 8
Pages 1167-78
Authors Tete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A
Title Crystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution.
Related PDB 1ff3
Related UniProtKB
[6]
Resource
Comments
Medline ID
PubMed ID 11311146
Journal Biochem J
Year 2001
Volume 355
Pages 819-25
Authors Petropoulos I, Mary J, Perichon M, Friguet B
Title Rat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging.
Related PDB
Related UniProtKB
[7]
Resource
Comments
Medline ID
PubMed ID 11430764
Journal J Biomol NMR
Year 2001
Volume 20
Pages 97-8
Authors Beraud S, Chambost JP, Bersch B, Gans P, Barras F, Marion D
Title Backbone H(N), N, Calpha, C' and Cbeta assignment of the 25 kDa peptide methionine sulfoxide reductase from Erwinia chrysanthemi.
Related PDB
Related UniProtKB
[8]
Resource
Comments
Medline ID
PubMed ID 11604533
Journal Protein Sci
Year 2001
Volume 10
Pages 2272-9
Authors Boschi-Muller S, Azza S, Branlant G
Title E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide.
Related PDB
Related UniProtKB
[9]
Resource
Comments
Medline ID
PubMed ID 11860363
Journal Curr Med Chem
Year 2002
Volume 9
Pages 385-409
Authors Vaughan MD, Sampson PB, Honek JF
Title Methionine in and out of proteins: targets for drug design.
Related PDB
Related UniProtKB
[10]
Resource
Comments
Medline ID
PubMed ID 12431100
Journal J Am Chem Soc
Year 2002
Volume 124
Pages 13709-15
Authors Beraud S, Bersch B, Brutscher B, Gans P, Barras F, Blackledge M
Title Direct structure determination using residual dipolar couplings: reaction-site conformation of methionine sulfoxide reductase in solution.
Related PDB
Related UniProtKB
[11]
Resource
Comments
Medline ID
PubMed ID 11812798
Journal J Biol Chem
Year 2002
Volume 277
Pages 12016-22
Authors Olry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van Dorsselear A, Branlant G
Title Characterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis.
Related PDB
Related UniProtKB
[12]
Resource
Comments
Medline ID
PubMed ID 11885278
Journal Methods Enzymol
Year 2002
Volume 348
Pages 249-59
Authors Davis DA, Newcomb FM, Moskovitz J, Fales HM, Levine RL, Yarchoan R
Title Reversible oxidation of HIV-2 protease.
Related PDB
Related UniProtKB
[13]
Resource
Comments
Medline ID
PubMed ID 11938352
Journal Nat Struct Biol
Year 2002
Volume 9
Pages 348-52
Authors Lowther WT, Weissbach H, Etienne F, Brot N, Matthews BW
Title The mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.
Related PDB
Related UniProtKB
[14]
Resource
Comments
Medline ID
PubMed ID 11807942
Journal Proteins
Year 2002
Volume 46
Pages 149-52
Authors Gladyshev VN
Title Thioredoxin and peptide methionine sulfoxide reductase: convergence of similar structure and function in distinct structural folds.
Related PDB
Related UniProtKB
[15]
Resource
Comments
Medline ID
PubMed ID 12837786
Journal J Bacteriol
Year 2003
Volume 185
Pages 4119-26
Authors Taylor AB, Benglis DM Jr, Dhandayuthapani S, Hart PJ
Title Structure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
Related PDB 1nwa
Related UniProtKB

Comments
The E.C. was transferred from 1.8.4.6 to 1.8.4.11.
This enzyme catalyzes two successive raections (see [1], [2], [4], [5], [9] & [15]):
(A) Reduction of L-methionine S-oxide.
(B) Reduction of active-site residues through oxidation of reduced thioredoxin.

Created Updated
2004-02-02 2009-02-26