A pH-dependent conformational change of NhaA Na+/H+ antiporter of Escherichia coli involves loop VIII-IX, plays a role in the pH response of the protein, and is maintained by the pure protein in dodecyl maltoside

Journal of Biological Chemistry

Volumn 274, Issue 35, 1999, Pages 24617-24624

  Gerchman, Yoram ^a   Rimon, Abraham ^a   Padan, Etana ^a  

^a HEBREW UNIVERSITY OF JERUSALEM   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CARRIER PROTEIN; MALTOSE; PROTON; PYRANOSIDE; SODIUM;

ARTICLE; CONFORMATIONAL TRANSITION; ESCHERICHIA COLI; MEMBRANE VESICLE; MUTAGENESIS; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DEGRADATION; PROTON SODIUM EXCHANGE;

AMINO ACID SEQUENCE; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; GLUCOSIDES; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; MUTATION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SEQUENCE ANALYSIS; SODIUM-HYDROGEN ANTIPORTER; TRYPSIN;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0033609818     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.274.35.24617     Document Type: Article

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