Structural and redox properties of the leaderless DsbE (CcmG) protein: Both active-site cysteines of the reduced form are involved in its function in the Escherichia coli periplasm

Biological Chemistry

Volumn 382, Issue 12, 2001, Pages 1679-1686

  Li, Qi ^a   Hu, Hong Yu ^a   Wang, Wei Qing ^a   Xu, Gen Jun ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

Active site cysteine; DsbE protein; Redox; Reduced structure; Thiol disulfide

Indexed keywords

CYSTEINE; CYTOCHROME C; DISULFIDE; INSULIN; OXIDOREDUCTASE; THIOL;

AMINO TERMINAL SEQUENCE; ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CYTOPLASM; ELECTRON TRANSPORT; ENZYME ACTIVE SITE; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; STRUCTURE ANALYSIS;

BINDING SITES; CIRCULAR DICHROISM; CYSTEINE; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; MOLECULAR WEIGHT; OXIDATION-REDUCTION; OXIDOREDUCTASES; PERIPLASM; PERIPLASMIC PROTEINS; PROTEIN FOLDING; SPECTROMETRY, FLUORESCENCE;

ESCHERICHIA COLI;

EID: 0035700860     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2001.203     Document Type: Article

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