Role of transmembrane segment 10 in efflux mediated by the staphylococcal multidrug transport protein QacA

Journal of Biological Chemistry

Volumn 281, Issue 2, 2006, Pages 792-799

  Xu, Zhiqiang ^a   O'Rourke, Brendon A ^a,b   Skurray, Ronald A ^a   Brown, Melissa H ^a  

^a UNIVERSITY OF SYDNEY   (Australia)

^b NSW DEPARTMENT OF PRIMARY INDUSTRIES   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; FLUORESCENCE; HYDROPHOBICITY; SOLVENTS; SUBSTRATES;

ANTIMICROBIAL COMPOUNDS; CYSTEINE-SCANNING; STAPHYLOCOCCAL MULTIDRUGS; SUBSTRATE BINDING;

PROTEINS;

4',6 DIAMIDINO 2 PHENYLINDOLE; AMINO ACID; ASPARTIC ACID; BACTERIAL PROTEIN; CARRIER PROTEIN; CYSTEINE; DIVALENT CATION; ETHIDIUM; MALEIMIDE DERIVATIVE; METHIONINE; MONOVALENT CATION; MUTANT PROTEIN; PROTEIN QACA; SOLVENT; UNCLASSIFIED DRUG; MALEIMIDE; QACA PROTEIN, STAPHYLOCOCCUS AUREUS;

ARTICLE; BINDING SITE; CONFORMATION; CONTROLLED STUDY; DNA FLANKING REGION; EFFUSION; MUTAGENESIS; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN EXPRESSION; PROTEIN SECONDARY STRUCTURE; STAPHYLOCOCCUS; AMINO ACID SEQUENCE; CELL MEMBRANE; CHEMISTRY; ESCHERICHIA COLI; FLUORESCENCE MICROSCOPY; KINETICS; METABOLISM; MOLECULAR GENETICS; MULTIDRUG RESISTANCE; MUTATION; PROTEIN CONFORMATION; PROTEIN TERTIARY STRUCTURE; PROTEIN TRANSPORT; STAPHYLOCOCCUS AUREUS; TRANSPORT AT THE CELLULAR LEVEL; WESTERN BLOTTING;

BACTERIA (MICROORGANISMS); STAPHYLOCOCCUS;

AMINO ACID SEQUENCE; ASPARTIC ACID; BACTERIAL PROTEINS; BINDING SITES; BIOLOGICAL TRANSPORT; BLOTTING, WESTERN; CELL MEMBRANE; CYSTEINE; DRUG RESISTANCE, MULTIPLE; ESCHERICHIA COLI; KINETICS; MALEIMIDES; MEMBRANE TRANSPORT PROTEINS; METHIONINE; MICROSCOPY, FLUORESCENCE; MOLECULAR SEQUENCE DATA; MUTAGENESIS; MUTATION; PHENOTYPE; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTEIN TRANSPORT; SOLVENTS; STAPHYLOCOCCUS AUREUS;

EID: 33644861768     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M508676200     Document Type: Article

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