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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
13
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pubmed:dateCreated |
1998-10-28
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pubmed:abstractText |
The entire lactose permease of Escherichia coli, a polytopic membrane transport protein that catalyzes beta-galactoside/H+ symport, has been subjected to Cys-scanning mutagenesis in order to determine which residues play an obligatory role in the mechanism and to create a library of mutants with a single-Cys residue at each position of the molecule for structure/function studies. Analysis of the mutants has led to the following: 1) only six amino acid side chains play an irreplaceable role in the transport mechanism; 2) positions where the reactivity of the Cys replacement is increased upon ligand binding are identified; 3) positions where the reactivity of the Cys replacement is decreased by ligand binding are identified; 4) helix packing, helix tilt, and ligand-induced conformational changes are determined by using the library of mutants in conjunction with a battery of site-directed techniques; 5) the permease is a highly flexible molecule; and 6) a working model that explains coupling between beta-galactoside and H+ translocation. structure-function relationships in polytopic membrane proteins.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/LacY protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Monosaccharide Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Protons,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Symporters,
http://linkedlifedata.com/resource/pubmed/chemical/lactose permease
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0892-6638
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1281-99
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9761772-Alkylation,
pubmed-meshheading:9761772-Amino Acid Sequence,
pubmed-meshheading:9761772-Antibodies, Monoclonal,
pubmed-meshheading:9761772-Bacterial Proteins,
pubmed-meshheading:9761772-Binding Sites,
pubmed-meshheading:9761772-Catalytic Domain,
pubmed-meshheading:9761772-Cysteine,
pubmed-meshheading:9761772-Escherichia coli,
pubmed-meshheading:9761772-Escherichia coli Proteins,
pubmed-meshheading:9761772-Glutamic Acid,
pubmed-meshheading:9761772-Ion Transport,
pubmed-meshheading:9761772-Membrane Proteins,
pubmed-meshheading:9761772-Membrane Transport Proteins,
pubmed-meshheading:9761772-Models, Molecular,
pubmed-meshheading:9761772-Molecular Sequence Data,
pubmed-meshheading:9761772-Monosaccharide Transport Proteins,
pubmed-meshheading:9761772-Mutagenesis, Site-Directed,
pubmed-meshheading:9761772-Protein Conformation,
pubmed-meshheading:9761772-Protein Structure, Secondary,
pubmed-meshheading:9761772-Protons,
pubmed-meshheading:9761772-Recombinant Fusion Proteins,
pubmed-meshheading:9761772-Structure-Activity Relationship,
pubmed-meshheading:9761772-Symporters
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pubmed:year |
1998
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pubmed:articleTitle |
Cys-scanning mutagenesis: a novel approach to structure function relationships in polytopic membrane proteins.
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pubmed:affiliation |
Howard Hughes Medical Institute, Departments of Physiology and Microbiology and Molecular Genetics, Molecular Biology Institute, University of California Los Angeles, Los Angeles, California 90024 1570.RonaldK@HHMI.UCLA.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Review,
Research Support, Non-U.S. Gov't
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