Staphylococcus aureus DsbA does not have a destabilizing disulfide: A new paradigm for bacterial oxidative folding

Journal of Biological Chemistry

Volumn 283, Issue 7, 2008, Pages 4261-4271

  Heras, Begoña ^a   Kurz, Mareike ^a   Jarrott, Russell ^a   Shouldice, Stephen R ^a   Frei, Patrick ^b   Robin, Gautier ^a   Čemažar, Maša ^a   Thöny Meyer, Linda ^c   Glockshuber, Rudi ^b   Martin, Jennifer L ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b ETH ZURICH   (Switzerland)

^c SWISS FEDERAL LABORATORIES FOR MATERIALS SCIENCE AND TECHNOLOGY   (Switzerland)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIOLOGY; BINDING SITES; CRYSTAL STRUCTURE; DIFFRACTIVE OPTICAL ELEMENTS; ESCHERICHIA COLI; PROTEIN FOLDING; PROTEINS;

ACTIVE SITES; BIOCHEMICAL ASSAYS; COMPLEMENTATION; DIFFERENT SUBSTRATES; DISULFIDE BONDS; EXTRACELLULAR; HELICAL DOMAINS; HYDROPHOBIC PATCHES; OXIDATIVE FOLDING; PERIPLASM; REDUCED FORMS; S. AUREUS; STAPHYLOCOCCUS AUREUS; THIOREDOXIN;

BACTERIA;

DISULFIDE; DISULFIDE ISOMERASE; DISULFIDE REDUCTASE; DSBA PROTEIN; THIOREDOXIN; UNCLASSIFIED DRUG; BACTERIAL PROTEIN; DSBB PROTEIN, BACTERIA; MEMBRANE PROTEIN;

AEROBIC METABOLISM; ARTICLE; CONTROLLED STUDY; CRYSTAL STRUCTURE; DISULFIDE BOND; ESCHERICHIA COLI; HYDROPHILICITY; NONHUMAN; OXIDATION REDUCTION POTENTIAL; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN STABILITY; SEQUENCE ANALYSIS; STAPHYLOCOCCUS AUREUS; THERMODYNAMICS; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; CRYSTALLIZATION; METABOLISM; MOLECULAR GENETICS; OXIDATIVE STRESS; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; POSIBACTERIA; STAPHYLOCOCCUS AUREUS;

AMINO ACID SEQUENCE; BACTERIAL PROTEINS; CRYSTALLIZATION; DISULFIDES; MEMBRANE PROTEINS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; OXIDATIVE STRESS; PROTEIN CONFORMATION; PROTEIN FOLDING; SEQUENCE HOMOLOGY, AMINO ACID; STAPHYLOCOCCUS AUREUS;

EID: 42949135118     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M707838200     Document Type: Article

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