Structure and mechanism of the lactose permease of Escherichia coli

Science

Volumn 301, Issue 5633, 2003, Pages 610-615

  Abramson, Jeff ^a   Smirnova, Irina ^b   Kasho, Vladimir ^b   Verner, Gillian ^b   Kaback, H Ronald ^b   Iwata, So ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

^b UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CONFORMATIONS; CRYSTAL STRUCTURE; ELECTROCHEMISTRY; ESCHERICHIA COLI; FREE ENERGY; ION EXCHANGE MEMBRANES;

CYTOPLASMS; ION GRADIENTS;

PROTEINS;

BETA DEXTRO GALACTOPYRANOSYL 1 THIO BETA DEXTRO GALACTOPYRANOSIDE; CARBOHYDRATE DERIVATIVE; LACTOSE; LACTOSE PERMEASE; UNCLASSIFIED DRUG;

MEMBRANE; PROTEIN;

ARTICLE; BACTERIAL METABOLISM; CONFORMATIONAL TRANSITION; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTON TRANSPORT;

AMINO ACID SUBSTITUTION; BINDING SITES; BIOLOGICAL TRANSPORT; CELL MEMBRANE; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HYDROGEN BONDING; HYDROPHOBICITY; ION TRANSPORT; LACTOSE; MEMBRANE TRANSPORT PROTEINS; MODELS, MOLECULAR; MONOSACCHARIDE TRANSPORT PROTEINS; MUTATION; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; PROTONS; SUBSTRATE SPECIFICITY; SYMPORTERS; THIOGALACTOSIDES;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI;

EID: 0041353145     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1088196     Document Type: Article

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39. Supported by the Biotechnology and Biological Sciences Research Council of the UK (S.I.) and in part by NIH grant DKS1131:08 (H.R.K.). We thank T. Tomizaki and C. Schulze-Briese at the Swiss Light Source and D. Flot, B. Shepard, and S. McSweeney at the European Synchrotron Radiation Facility for technical assistance; members of the Iwata and Kaback laboratories for their support; B. Byrne for critically reading the manuscript; and M. Iwata for data collection. The coordinates for the native LacY and the TDG complex have been deposited in the Protein Data Bank (entries 1PV6 and 1PV7, respectively).