Site-directed spin labeling and chemical crosslinking demonstrate that helix V is close to helices VII and VIII in the lactose permease of Escherichia coli

Proceedings of the National Academy of Sciences of the United States of America

Volumn 93, Issue 19, 1996, Pages 10123-10127

  Wu, Jianhua ^a   Voss, John ^a   Hubbell, Wayne L ^b   Kaback, H Ronald ^a,c  

^a HOWARD HUGHES MEDICAL INSTITUTE   (United States)

^b JULES STEIN EYE INSTITUTE   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Cys less permease; double Cys mutants; electron paramagnetic resonance; helix packing; spin spin interactions

Indexed keywords

BACTERIAL ENZYME; LACTOSE PERMEASE;

ARTICLE; ELECTRON SPIN RESONANCE; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN CROSS LINKING; SPIN LABELING;

AMINO ACID SEQUENCE; BIOTIN; CELL MEMBRANE; CYSTEINE; CYTOPLASM; ELECTRON SPIN RESONANCE SPECTROSCOPY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; ETHYLMALEIMIDE; MEMBRANE TRANSPORT PROTEINS; MODELS, STRUCTURAL; MOLECULAR SEQUENCE DATA; MONOSACCHARIDE TRANSPORT PROTEINS; MUTAGENESIS, SITE-DIRECTED; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPIN LABELS; SYMPORTERS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0029789304     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.93.19.10123     Document Type: Article

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