Cysteine Cross-linking Defines Part of the Dimer and B/C Domain Interface of the Escherichia coli Mannitol Permease

Journal of Biological Chemistry

Volumn 276, Issue 16, 2001, Pages 12756-12763

  Van Montfort, Bart A ^a   Schuurman Wolters, Gea K ^a   Duurkens, Ria H ^a   Mensen, Robert ^a   Poolman, Bert ^a   Robillard, George T ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

CROSSLINKING; CYTOLOGY; DIMERS; ELECTROPHORESIS; ESCHERICHIA COLI; MASS SPECTROMETRY; OXIDATION;

CYTOPLASM;

ENZYMES;

1,10 PHENANTHROLINE COPPER; BACTERIAL ENZYME; CYSTEINE; DIMALEIMIDE; DIMER; IMIDE; MANNITOL PERMEASE; UNCLASSIFIED DRUG; 1,10 PHENANTHROLINE; 1,10-PHENANTHROLINE; COPPER; CROSS LINKING REAGENT; DISULFIDE; MALEIMIDE DERIVATIVE; MANNITOL; PHENANTHROLINE DERIVATIVE; PHOSPHOENOLPYRUVATE MANNITOL PHOSPHOTRANSFERASE; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE; PHOSPHOENOLPYRUVATE-MANNITOL PHOSPHOTRANSFERASE; RECOMBINANT PROTEIN;

AMINO ACID SEQUENCE; ARTICLE; CROSS LINKING; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STRUCTURE; ESCHERICHIA COLI; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; OXIDATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; AMINO ACID SUBSTITUTION; BINDING SITE; CHEMISTRY; DIMERIZATION; ENZYMOLOGY; MASS SPECTROMETRY; METABOLISM; OXIDATION REDUCTION REACTION; PHOSPHORYLATION; SITE DIRECTED MUTAGENESIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

AMINO ACID SUBSTITUTION; BINDING SITES; COPPER; CROSS-LINKING REAGENTS; CYSTEINE; DIMERIZATION; DISULFIDES; ESCHERICHIA COLI; MALEIMIDES; MANNITOL; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PHENANTHROLINES; PHOSPHOENOLPYRUVATE SUGAR PHOSPHOTRANSFERASE SYSTEM; PHOSPHORYLATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EID: 0035918216     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010728200     Document Type: Article

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