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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2011-3-8
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pubmed:abstractText |
In total, 59 single Cys-replacement mutants in helix VII and helix X of the lactose permease of Escherichia coli were subjected to site-directed fluorescence labeling in right-side-out membrane vesicles to complete the testing of Cys accessibility or reactivity. For both helices, accessibility/reactivity is relatively low at the level of the sugar-binding site where the helices are tightly packed. However, labeling of Cys substitutions in helix VII with tetramethylrhodamine-5-maleimide decreases from the middle toward the cytoplasmic end and increases toward the periplasmic end. Helix X is labeled mainly on the side facing the central hydrophilic cavity with relatively small or no changes in the presence of ligand. In contrast, sugar binding causes a significant increase in accessibility/reactivity at the periplasmic end of helix VII. When considered with similar findings from N-ethylmaleimide alkylation studies, the results confirm and extend support for the alternating access model.
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pubmed:grant |
http://linkedlifedata.com/resource/pubmed/grant/DK051131,
http://linkedlifedata.com/resource/pubmed/grant/DK069463,
http://linkedlifedata.com/resource/pubmed/grant/GM073210,
http://linkedlifedata.com/resource/pubmed/grant/GM074929,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-04,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-05,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-06,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-07,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-08,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-09,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-10,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-11,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-12,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-13,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-14,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-15,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK051131-16,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK069463-01,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK069463-02,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK069463-03,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK069463-04,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK069463-05A2,
http://linkedlifedata.com/resource/pubmed/grant/R01 DK069463-06,
http://linkedlifedata.com/resource/pubmed/grant/R56 DK069463-05A1
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1520-4995
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
50
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1634-40
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pubmed:meshHeading |
pubmed-meshheading:21254783-Alkylation,
pubmed-meshheading:21254783-Biological Transport,
pubmed-meshheading:21254783-Klebsiella pneumoniae,
pubmed-meshheading:21254783-Membrane Transport Proteins,
pubmed-meshheading:21254783-Models, Biological,
pubmed-meshheading:21254783-Models, Molecular,
pubmed-meshheading:21254783-Mutation,
pubmed-meshheading:21254783-Protein Structure, Tertiary
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pubmed:year |
2011
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pubmed:articleTitle |
Site-directed alkylation studies with LacY provide evidence for the alternating access model of transport.
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pubmed:affiliation |
Department of Physiology, University of California, Los Angeles, California 90095, United States.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, N.I.H., Extramural
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