Cd2+ and the N-terminal metal-binding domain protect the putative membranous CPC motif of the Cd2+-ATPase of Listeria monocytogenes

Biochemical Journal

Volumn 369, Issue 3, 2003, Pages 681-685

  Bal, Nathalie ^a   Wu, Chen Chou ^a   Catty, Patrice ^a   Guillain, Florent ^a   Mintz, Elisabeth ^a  

^a CEA GRENOBLE   (France)

Author keywords

CadA; CXXC; Heavy metal; P type ATPase; Transport site

Indexed keywords

ALKYLATION; AMINO ACIDS; BIOLOGICAL MEMBRANES; ENZYMES;

MONOCYTOGENES;

BIOCHEMISTRY;

ADENOSINE TRIPHOSPHATASE; AMINO ACID; CADMIUM; CADMIUM ADENOSINE TRIPHOSPHATASE; CYSTEINYLPROLYLCYSTEINE; N ETHYLMALEIMIDE; UNCLASSIFIED DRUG; CADMIUM TRANSLOCATING ATPASE; CYSTEINE; THIOL REAGENT;

ALKYLATION; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; ENZYME ACTIVITY; ION TRANSPORT; LISTERIA MONOCYTOGENES; NONHUMAN; PHOSPHORYLATION; PRIORITY JOURNAL; PROTEIN DOMAIN; ACTIVE TRANSPORT; CELL MEMBRANE; CHEMISTRY; ENZYMOLOGY; GENETICS; METABOLISM; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE;

LISTERIA; LISTERIA MONOCYTOGENES; POSIBACTERIA;

ADENOSINE TRIPHOSPHATASES; AMINO ACID MOTIFS; BIOLOGICAL TRANSPORT, ACTIVE; CADMIUM; CELL MEMBRANE; CYSTEINE; ETHYLMALEIMIDE; LISTERIA MONOCYTOGENES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; SULFHYDRYL REAGENTS;

EID: 0037289803     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20021416     Document Type: Article

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