Covalent modification of cysteine 193 impairs ATPase function of nucleotide-binding domain of a Candida drug efflux pump

Biochemical and Biophysical Research Communications

Volumn 310, Issue 3, 2003, Pages 869-875

  Jha, Sudhakar ^a   Karnani, Neerja ^a   Lynn, Andrew M ^a   Prasad, Rajendra ^a  

^a JAWAHARLAL NEHRU UNIVERSITY   (India)

Author keywords

ABC transporter; ATP hydrolysis; ATPase; Candida albicans; Cdr1p; Covalent modification; Cysteine; N ethylmaleimide; Nucleotide binding domain; Structural homology

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CYSTEINE; DIVALENT CATION; GENE PRODUCT; IODOACETIC ACID; N ETHYLMALEIMIDE; NUCLEOTIDE; PROTEIN CDR1P; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ARTICLE; BINDING SITE; CANDIDA; CATALYSIS; CONTROLLED STUDY; COVALENT BOND; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME INHIBITION; ENZYME MECHANISM; ENZYME STRUCTURE; HYDROLYSIS; MOLECULAR INTERACTION; MOLECULAR MODEL; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN MODIFICATION; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; VALIDATION PROCESS;

CANDIDA; CANDIDA ALBICANS;

EID: 0141868865     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.094     Document Type: Article

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