Helix packing in the lactose permease of Escherichia coli: Localization of helix VI

Journal of Molecular Biology

Volumn 312, Issue 1, 2001, Pages 69-77

  Guan, Lan ^a   Weinglass, Adam B ^a   Kaback, H Ronald ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Bioenergetics; Cross linking; Membrane proteins; Structure; Transport

Indexed keywords

ARGININE; BETA DEXTRO GALACTOPYRANOSYL 1 THIO BETA DEXTRO GALACTOPYRANOSIDE; CYSTEINE; DNA; GLUTAMINE; HISTIDINE; LACTOSE PERMEASE; MEMBRANE PROTEIN; PYRANOSIDE; REAGENT; UNCLASSIFIED DRUG;

ARTICLE; BINDING AFFINITY; CYTOPLASM; DNA HELIX; ENZYME ACTIVE SITE; ENZYME LOCALIZATION; ENZYME STRUCTURE; ESCHERICHIA COLI; GENE CONSTRUCT; MEMBRANE BINDING; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN TERTIARY STRUCTURE;

ESCHERICHIA COLI;

EID: 0035823221     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2001.4933     Document Type: Article

References (39)

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14. Site-directed sulfhydryl labeling of the lactose permease of Escherichia coli: Helix II
15. Unraveling the mechanism of lactose permease of Escherichia coli
16. Intramolecular dislocation of the COOH terminus of the lac carrier protein in reconstituted proteoliposomes
17. Nitroxide scanning electron paramagnetic resonance of helices IV, V and the intervening loop in the lactose permease of Escherichia coli
18. Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage
19. 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
20. Tertiary contacts of helix V in the lactose permease determined by site-directed chemical crosslinking in situ
21. Helix packing in the lactose permease of Escherichia coli: Distances between site-directed nitroxides and a lanthanide
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23. Isolation and nucleotide sequencing of lactose carrier mutants that transport maltose
24. Identification of valine 177 as a mutation altering specificity for transport of sugars by the Escherichia coli lactose carrier. Enhanced specificity for sucrose and maltose
25. Isolation of lactose permease mutants which recognize arabinose
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27. Functional estimation of loop-helix boundaries in the lactose permease of Escherichia coli by single amino acid deletion analysis
28. The role of helix VIII in the lactose permease of Escherichia coli. II. Site-directed sulfhydryl modification
29. Cysteine-scanning mutagenesis of helix IV and the adjoining loops in the lactose permease of Escherichia coli: Glu126 and Arg144 are essential
30. The substrate binding site in the lactose permease of Escherichia coli
31. Characterization of Glu126 and Arg144, two residues that are indispensable for substrate binding in the lactose permease of Escherichia coli
32. Ligand recognition by the lactose permease of Escherichia coli: Specificity and affinity are defined by distinct structural elements of galactopyranosides
33. Interaction between residues Glu269 (Helix VIII) and His322 (Helix X) of the lactose permease of Escherichia coli is essential for substrate binding
34. Construction of a functional lactose permease devoid of cysteine residues
35. DNA sequencing with chain-terminating inhibitors
36. Helix proximity and ligand-induced conformational changes in the lactose permease of Escherichia coli determined by site-directed chemical crosslinking
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38. Mechanisms of active transport in isolated membrane vesicles. 2. The coupling of reduced phenazine methosulfate to the concentrative uptake of β-galactosides and amino acids
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