EzCatDB: S00277

DB codeS00277
CATH domainDomain 13.30.1060.10Catalytic domain
E.C.1.8.4.11
CSA1ff3,1fva
MACiEM0122

CATH domainRelated DB codes (homologues)
3.30.1060.10S00523

Enzyme Name
Swiss-protKEGG

P0A744P54149
Protein namePeptide methionine sulfoxide reductase msrAPeptide methionine sulfoxide reductasepeptide-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
SynonymsProtein-methionine-S-oxide reductase
EC 1.8.4.11
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase
EC 1.8.4.11
Protein-methionine-S-oxide reductase
Peptide-methionine (S)-S-oxide reductase
Peptide Met(O) reductase


Swiss-prot:Accession NumberP0A744P54149
Entry nameMSRA_ECOLIMSRA_BOVIN
ActivityPeptide-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.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.
Subunit

Subcellular location

Cofactor



SubstratesProductsintermediates
KEGG-idC03895C00342C15999C03023C00343C00001C00073
CompoundPeptide-L-methionine (S)-S-oxideReduced thioredoxinL-methionine (S)-S-oxidePeptide-L-methionineOxidized thioredoxinH2OL-methionine
Typepeptide/protein,sulfoxide groupamide group,carbohydrate,peptide/protein,sulfhydryl groupamino acids,sulfoxide grouppeptide/protein,sulfide groupamide group,carbohydrate,disulfide bond,peptide/proteinH2Oamino acids,sulfide group
1ff3AUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1ff3BUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1ff3CUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1fvaAUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1fvaBUnboundUnboundUnboundUnboundUnbound
UnboundUnbound
1fvgAUnboundAnalogue:DTTUnboundUnboundUnbound
UnboundIntermediate-analogue:DTT

Active-site residues
resource
PDB;1fvg
pdbCatalytic residuesModified residuescomment
1ff3A      ;TYR  82;GLU  94;TYR 134;CYS 198;CYS 206
CAS 51

1ff3B      ;TYR  82;GLU  94;TYR 134;       ;       
CAS 51
invisible 195-211
1ff3C      ;TYR  82;GLU  94;TYR 134;       ;       
CAS 51
invisible 193-211
1fvaACYS 72;TYR 103;GLU 115;TYR 155;CYS 218;CYS 227


1fvaBCYS 72;TYR 103;GLU 115;TYR 155;CYS 218;CYS 227


1fvgACYS 72;TYR 103;GLU 115;TYR 155;CYS 218;       

truncation 219-228

References for Catalytic Mechanism
ReferencesSectionsNo. 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]
CommentsX-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS)
Medline ID20519025
PubMed ID11063566
JournalBiochemistry
Year2000
Volume39
Pages13307-12
AuthorsLowther WT, Brot N, Weissbach H, Matthews BW
TitleStructure and mechanism of peptide methionine sulfoxide reductase, an "anti-oxidation" enzyme.
Related PDB1fva,1fvg
Related Swiss-protP54149
[2]
PubMed ID10964927
JournalJ Biol Chem
Year2000
Volume275
Pages35908-13
AuthorsBoschi-Muller S, Azza S, Sanglier-Cianferani S, Talfournier F, Van Dorsselear A, Branlant G
TitleA sulfenic acid enzyme intermediate is involved in the catalytic mechanism of peptide methionine sulfoxide reductase from Escherichia coli.
[3]
PubMed ID10799493
JournalJ Biol Chem
Year2000
Volume275
Pages14167-72
AuthorsMoskovitz J, Poston JM, Berlett BS, Nosworthy NJ, Szczepanowski R, Stadtman ER
TitleIdentification and characterization of a putative active site for peptide methionine sulfoxide reductase (MsrA) and its substrate stereospecificity.
[4]
PubMed ID10841552
JournalProc Natl Acad Sci U S A
Year2000
Volume97
Pages6463-8
AuthorsLowther WT, Brot N, Weissbach H, Honek JF, Matthews BW
TitleThiol-disulfide exchange is involved in the catalytic mechanism of peptide methionine sulfoxide reductase.
[5]
PubMed ID11080639
JournalStructure Fold Des
Year2000
Volume8
Pages1167-78
AuthorsTete-Favier F, Cobessi D, Boschi-Muller S, Azza S, Branlant G, Aubry A
TitleCrystal structure of the Escherichia coli peptide methionine sulphoxide reductase at 1.9 A resolution.
Related PDB1ff3
[6]
PubMed ID11311146
JournalBiochem J
Year2001
Volume355
Pages819-25
AuthorsPetropoulos I, Mary J, Perichon M, Friguet B
TitleRat peptide methionine sulphoxide reductase: cloning of the cDNA, and down-regulation of gene expression and enzyme activity during aging.
[7]
PubMed ID11430764
JournalJ Biomol NMR
Year2001
Volume20
Pages97-8
AuthorsBeraud S, Chambost JP, Bersch B, Gans P, Barras F, Marion D
TitleBackbone H(N), N, Calpha, C' and Cbeta assignment of the 25 kDa peptide methionine sulfoxide reductase from Erwinia chrysanthemi.
[8]
PubMed ID11604533
JournalProtein Sci
Year2001
Volume10
Pages2272-9
AuthorsBoschi-Muller S, Azza S, Branlant G
TitleE. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide.
[9]
PubMed ID11860363
JournalCurr Med Chem
Year2002
Volume9
Pages385-409
AuthorsVaughan MD, Sampson PB, Honek JF
TitleMethionine in and out of proteins: targets for drug design.
[10]
PubMed ID12431100
JournalJ Am Chem Soc
Year2002
Volume124
Pages13709-15
AuthorsBeraud S, Bersch B, Brutscher B, Gans P, Barras F, Blackledge M
TitleDirect structure determination using residual dipolar couplings: reaction-site conformation of methionine sulfoxide reductase in solution.
[11]
PubMed ID11812798
JournalJ Biol Chem
Year2002
Volume277
Pages12016-22
AuthorsOlry A, Boschi-Muller S, Marraud M, Sanglier-Cianferani S, Van Dorsselear A, Branlant G
TitleCharacterization of the methionine sulfoxide reductase activities of PILB, a probable virulence factor from Neisseria meningitidis.
[12]
PubMed ID11885278
JournalMethods Enzymol
Year2002
Volume348
Pages249-59
AuthorsDavis DA, Newcomb FM, Moskovitz J, Fales HM, Levine RL, Yarchoan R
TitleReversible oxidation of HIV-2 protease.
[13]
PubMed ID11938352
JournalNat Struct Biol
Year2002
Volume9
Pages348-52
AuthorsLowther WT, Weissbach H, Etienne F, Brot N, Matthews BW
TitleThe mirrored methionine sulfoxide reductases of Neisseria gonorrhoeae pilB.
[14]
PubMed ID11807942
JournalProteins
Year2002
Volume46
Pages149-52
AuthorsGladyshev VN
TitleThioredoxin and peptide methionine sulfoxide reductase: convergence of similar structure and function in distinct structural folds.
[15]
PubMed ID12837786
JournalJ Bacteriol
Year2003
Volume185
Pages4119-26
AuthorsTaylor AB, Benglis DM Jr, Dhandayuthapani S, Hart PJ
TitleStructure of Mycobacterium tuberculosis methionine sulfoxide reductase A in complex with protein-bound methionine.
Related PDB1nwa

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.

createdupdated
2004-02-022009-02-26


Copyright: Nozomi Nagano, JST & CBRC-AIST
Funded by PRESTO/Japan Science and Technology Corporation (JST) (December 2001 - November 2004)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2006)
Funded by Grant-in-Aid for Scientific Research (B)/Japan Society for the Promotion of Science (JSPS) (April 2005 - March 2008)
Funded by BIRD/Japan Science and Technology Corporation (JST) (September 2005 - September 2010)
Funded by BIRD/Japan Science and Technology Corporation (JST) (October 2007 - September 2010)
Funded by Grant-in-Aid for Publication of Scientific Research Results/Japan Society for the Promotion of Science (JSPS) (April 2011 - March 2012)

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