Methionine Sulfoxide Reductase B Displays a High Level of Flexibility

Journal of Molecular Biology

Volumn 394, Issue 1, 2009, Pages 83-93

  Ranaivoson, Fanomezana M ^a   Neiers, Fabrice ^b   Kauffmann, Brice ^a,c   Boschi Muller, Sandrine ^b   Branlant, Guy ^b   Favier, Frédérique ^a  

^a Nancy University CNRS   (France)

^b Biopôle de l Université de Lorraine   (France)

^c INSTITUT EUROPÉEN DE CHIMIE ET BIOLOGIE   (France)

Author keywords

conformational change; disulfide bond formation; flexibility; methionine sulfoxide reductase B; X ray structure

Indexed keywords

METHIONINE SULFOXIDE REDUCTASE B; THIOREDOXIN;

ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ACTIVE SITE; ENZYME METABOLISM; ENZYME STABILITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; NEISSERIA MENINGITIDIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; X RAY DIFFRACTION; XANTHOMONAS CAMPESTRIS;

NEISSERIA MENINGITIDIS; XANTHOMONAS CAMPESTRIS;

AMINO ACID SEQUENCE; BIOCATALYSIS; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; METHIONINE SULFOXIDE REDUCTASES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NEISSERIA MENINGITIDIS; OXIDATION-REDUCTION; OXIDOREDUCTASES; PLIABILITY; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ALIGNMENT; XANTHOMONAS CAMPESTRIS;

EID: 70350271424     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2009.08.073     Document Type: Article

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