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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2011-4-18
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pubmed:abstractText |
The Leu294 residue in the cytoplasmic neck of Thermotoga maritima CorA is considered to be the main gate for Mg2+ transport. We created three site-directed mutants at this position: in the Leu294Asp and Leu294Gly mutants we observed a defect in closing of the pore, while in the Leu294Arg mutant not only gating, but also the regulation of Mg2+ uptake was affected. Our results confirmed the importance of the Leu294 for gating of Mg2+ transport and in addition revealed the influence of the charge and structural features of the amino acid residues on the gating mechanism.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-10748031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-12628916,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-15268937,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-16598263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-16857941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-16902408,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-18276588,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-20197031,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-4960404,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-8314774,
http://linkedlifedata.com/resource/pubmed/commentcorrection/21074514-9622348
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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 |
Jun
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:copyrightInfo |
Copyright © 2010 Elsevier B.V. All rights reserved.
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pubmed:issnType |
Print
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pubmed:volume |
1808
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1587-91
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pubmed:dateRevised |
2011-7-28
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pubmed:meshHeading |
pubmed-meshheading:21074514-Amino Acid Substitution,
pubmed-meshheading:21074514-Aspartic Acid,
pubmed-meshheading:21074514-Bacterial Proteins,
pubmed-meshheading:21074514-Blotting, Western,
pubmed-meshheading:21074514-Cation Transport Proteins,
pubmed-meshheading:21074514-Glycine,
pubmed-meshheading:21074514-Hydrophobic and Hydrophilic Interactions,
pubmed-meshheading:21074514-Ion Transport,
pubmed-meshheading:21074514-Leucine,
pubmed-meshheading:21074514-Magnesium,
pubmed-meshheading:21074514-Models, Molecular,
pubmed-meshheading:21074514-Mutagenesis, Site-Directed,
pubmed-meshheading:21074514-Mutation,
pubmed-meshheading:21074514-Protein Conformation,
pubmed-meshheading:21074514-Thermotoga maritima
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pubmed:year |
2011
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pubmed:articleTitle |
Functional analysis of the conserved hydrophobic gate region of the magnesium transporter CorA.
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pubmed:affiliation |
Department of Microbiology, Immunobiology and Genetics, Max F. Perutz Laboratories, University of Vienna, Dr. Bohrgasse 9/4, A-1030 Vienna, Austria.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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