A histidine-rich metal binding domain at the N terminus of Cu, Zn-superoxide dismutases from pathogenic bacteria. A novel strategy for metal chaperoning

Journal of Biological Chemistry

Volumn 276, Issue 32, 2001, Pages 30315-30325

  Battistoni, Andrea ^a   Pacello, Francesca ^a   Mazzetti, Anna Paola ^a   Capo, Concetta ^a   Kroll, J Simon ^b   Langford, Paul R ^b   Sansone, Assunta ^b   Donnarumma, Giovanna ^c   Valenti, Piera ^c   Rotilio, Giuseppe ^a  

^a UNIVERSITY OF ROME TOR VERGATA   (Italy)

^b IMPERIAL COLLEGE SCHOOL OF MEDICINE   (United Kingdom)

^c UNIVERSITY OF NAPLES FEDERICO II   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

AFFINITY CHROMATOGRAPHY; BACTERIOLOGY; CATALYSIS; CONFORMATIONS; DIMERS; ENZYME KINETICS;

INTERMOLECULAR PATHWAYS;

BIOCHEMISTRY;

CHAPERONE; COPPER; COPPER ZINC SUPEROXIDE DISMUTASE; DIMER; EDETIC ACID; HISTIDINE; METAL; PROTEIN; PROTEINASE; SUPEROXIDE DISMUTASE;

AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME SUBUNIT; HAEMOPHILUS DUCREYI; HAEMOPHILUS PARAINFLUENZAE; HUMAN; HUMAN CELL; IMMOBILIZED METAL AFFINITY CHROMATOGRAPHY; METAL BINDING; MOUSE; NONHUMAN; PHAGOCYTE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN PURIFICATION; AMINO ACID SEQUENCE; ANIMAL; BINDING SITE; CHEMISTRY; CHROMATOGRAPHY; DIMERIZATION; ENZYMOLOGY; HAEMOPHILUS INFLUENZAE; KINETICS; MACROPHAGE; METABOLISM; MOLECULAR GENETICS; PATHOGENICITY; PHAGOCYTOSIS; PLASMID; PROTEIN BINDING; PROTEIN TERTIARY STRUCTURE; SEQUENCE HOMOLOGY; TIME;

ANIMALIA; HAEMOPHILUS; HAEMOPHILUS DUCREYI; HAEMOPHILUS PARAINFLUENZAE;

AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; CHROMATOGRAPHY; COPPER; DIMERIZATION; EDETIC ACID; ENDOPEPTIDASES; HAEMOPHILUS DUCREYI; HAEMOPHILUS INFLUENZAE; HISTIDINE; HUMANS; KINETICS; MACROPHAGES; MICE; MOLECULAR SEQUENCE DATA; PHAGOCYTOSIS; PLASMIDS; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUPEROXIDE DISMUTASE; TIME FACTORS;

EID: 0035839491     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M010527200     Document Type: Article

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