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rdf:type |
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lifeskim:mentions |
umls-concept:C0022896,
umls-concept:C0026377,
umls-concept:C0449911,
umls-concept:C1145667,
umls-concept:C1167622,
umls-concept:C1705273,
umls-concept:C1705274,
umls-concept:C1705275,
umls-concept:C2349209,
umls-concept:C2825311,
umls-concept:C2827501
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pubmed:issue |
3
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pubmed:dateCreated |
2000-4-7
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pubmed:databankReference |
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pubmed:abstractText |
Crystal structures of the Lac repressor, with and without isopropyithiogalactoside (IPTG), and the repressor bound to operator have provided a model for how the binding of the inducer reduces the affinity of the repressor for the operator. However, because of the low resolution of the operator-bound structure (4.8 A), the model for the allosteric transition was presented in terms of structural elements rather than in terms of side chain interactions. Here we have constructed a dimeric Lac repressor and determined its structure at 2.6 A resolution in complex with a symmetric operator and the anti-inducer orthonitrophenylfucoside (ONPF). The structure enables the induced (IPTG-bound) and repressed (operator-bound) conformations of the repressor to be compared in atomic detail. An extensive network of interactions between the DNA-binding and core domains of the repressor suggests a possible mechanism for the allosteric transition.
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pubmed:commentsCorrections |
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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/2-nitrophenyl-beta-fucoside,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Escherichia coli Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycosides,
http://linkedlifedata.com/resource/pubmed/chemical/Isopropyl Thiogalactoside,
http://linkedlifedata.com/resource/pubmed/chemical/Lac Repressors,
http://linkedlifedata.com/resource/pubmed/chemical/LacI protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
7
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
209-14
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10700279-Allosteric Regulation,
pubmed-meshheading:10700279-Bacterial Proteins,
pubmed-meshheading:10700279-Binding Sites,
pubmed-meshheading:10700279-Crystallization,
pubmed-meshheading:10700279-Crystallography, X-Ray,
pubmed-meshheading:10700279-DNA,
pubmed-meshheading:10700279-DNA-Binding Proteins,
pubmed-meshheading:10700279-Dimerization,
pubmed-meshheading:10700279-Escherichia coli,
pubmed-meshheading:10700279-Escherichia coli Proteins,
pubmed-meshheading:10700279-Glycosides,
pubmed-meshheading:10700279-Hydrogen Bonding,
pubmed-meshheading:10700279-Isopropyl Thiogalactoside,
pubmed-meshheading:10700279-Lac Repressors,
pubmed-meshheading:10700279-Models, Molecular,
pubmed-meshheading:10700279-Molecular Sequence Data,
pubmed-meshheading:10700279-Nucleic Acid Conformation,
pubmed-meshheading:10700279-Operator Regions, Genetic,
pubmed-meshheading:10700279-Protein Conformation,
pubmed-meshheading:10700279-Repressor Proteins,
pubmed-meshheading:10700279-Sequence Deletion,
pubmed-meshheading:10700279-Static Electricity,
pubmed-meshheading:10700279-Structure-Activity Relationship
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pubmed:year |
2000
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pubmed:articleTitle |
A closer view of the conformation of the Lac repressor bound to operator.
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pubmed:affiliation |
The Johnson Foundation and Department of Biochemistry and Biophysics, University of Pennsylvania School of Medicine, 37th and Hamilton walk, Philadelphia, Pennsylvania 19102-6059, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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