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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
50
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pubmed:dateCreated |
2009-12-16
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pubmed:abstractText |
The Cu(I) sensor Mycobacterium tuberculosis CsoR is a founding member of a new metalloregulatory protein family. Here we show that two "atom" substitutions of the Nepsilon2 face of a Cu(I) coordinating histidine-61 allosterically uncouple Cu(I) and DNA binding, with no effect on Cu(I) binding affinity and coordination structure. A model analogous to the allosteric switch mechanism in Staphylococcus aureus CzrA, a zinc sensor protein with a completely different fold, is proposed.
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1520-5126
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
23
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pubmed:volume |
131
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18044-5
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pubmed:dateRevised |
2011-8-29
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pubmed:meshHeading |
pubmed-meshheading:19928961-Allosteric Regulation,
pubmed-meshheading:19928961-Allosteric Site,
pubmed-meshheading:19928961-Amino Acid Substitution,
pubmed-meshheading:19928961-Bacterial Proteins,
pubmed-meshheading:19928961-Copper,
pubmed-meshheading:19928961-DNA-Binding Proteins,
pubmed-meshheading:19928961-Histidine,
pubmed-meshheading:19928961-Hydrogen Bonding,
pubmed-meshheading:19928961-Models, Molecular,
pubmed-meshheading:19928961-Mycobacterium tuberculosis
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pubmed:year |
2009
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pubmed:articleTitle |
Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor.
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pubmed:affiliation |
Department of Chemistry, Indiana University, Bloomington, Indiana 47405-7102, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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