The nucleotide-binding domain of the Zn2+-transporting P-type ATPase from Escherichia coli carries a glycine motif that may be involved in binding of ATP

Biochemical Journal

Volumn 377, Issue 1, 2004, Pages 95-105

  Okkeri, Juha ^a   Laakkonen, Liisa ^b   Haltia, Tuomas ^a  

^a UNIVERSITY OF HELSINKI   (Finland)

^b UNIVERSITY OF HELSINKI   (Finland)

Author keywords

Copper; Metal ion transport; Nucleotide binding domain; P1 type ATPase; Wilson disease

Indexed keywords

ADENOSINETRIPHOSPHATE; DISEASES; ESCHERICHIA COLI; MUTAGENESIS;

PHOSPHORYLATION;

ENZYME KINETICS;

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; GLUTAMIC ACID; GLYCINE; HISTIDINE; MUTANT PROTEIN; NUCLEOTIDE BINDING PROTEIN; SERINE; ZINC ION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING ASSAY; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME BINDING; ENZYME DEFECT; ENZYME PHOSPHORYLATION; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; GENE MUTATION; ION TRANSPORT; MOLECULAR MODEL; MUTAGENESIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; SARCOPLASMIC RETICULUM;

ADENOSINE TRIPHOSPHATASES; ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BINDING SITES; ESCHERICHIA COLI; GLYCINE; HISTIDINE; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEOTIDES; PHOSPHORYLATION; PROTEIN STRUCTURE, TERTIARY; SEQUENCE ALIGNMENT; ZINC;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA; PROKARYOTA;

EID: 1642535324     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20030740     Document Type: Article

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