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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
21
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pubmed:dateCreated |
2002-5-20
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pubmed:databankReference |
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pubmed:abstractText |
Members of the IclR family of transcription regulators modulate signal-dependent expression of genes involved in carbon metabolism in bacteria and archaea. The Thermotoga maritima TM0065 gene codes for a protein (TM-IclR) that is homologous to the IclR family. We have determined the crystal structure of TM-IclR at 2.2 A resolution using MAD phasing and synchrotron radiation. The protein is composed of two domains: the N-terminal DNA-binding domain contains the winged helix-turn-helix motif, and the C-terminal presumed regulatory domain is involved in binding signal molecule. In a proposed signal-binding site, a bound Zn(2+) ion was found. In the crystal, TM-IclR forms a dimer through interactions between DNA-binding domains. In the dimer, the DNA-binding domains are 2-fold related, but the dimer is asymmetric with respect to the orientation of signal-binding domains. Crystal packing analysis showed that TM-IclR dimers form a tetramer through interactions exclusively by signal-binding domains. A model is proposed for binding of IclR-like factors to DNA, and it suggests that signal-dependent transcription regulation is accomplished by affecting an oligomerization state of IclR and therefore its affinity for DNA target.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-10497029,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-10592242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-10706293,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-10913096,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-11004161,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-11420439,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-11731804,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-1545709,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-2001680,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-2185227,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-7033207,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-7792597,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-7881904,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8052126,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8107132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8332212,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8603061,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8682810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8755903,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8831795,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-8844850,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-9096308,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-9466913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-9748437,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-9757107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/11877432-9826648
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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 |
May
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
24
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pubmed:volume |
277
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
19183-90
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pubmed:dateRevised |
2011-9-26
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pubmed:meshHeading |
pubmed-meshheading:11877432-Amino Acid Sequence,
pubmed-meshheading:11877432-Bacterial Proteins,
pubmed-meshheading:11877432-Base Sequence,
pubmed-meshheading:11877432-Binding Sites,
pubmed-meshheading:11877432-Cloning, Molecular,
pubmed-meshheading:11877432-Crystallography, X-Ray,
pubmed-meshheading:11877432-DNA, Bacterial,
pubmed-meshheading:11877432-Escherichia coli Proteins,
pubmed-meshheading:11877432-Models, Molecular,
pubmed-meshheading:11877432-Molecular Sequence Data,
pubmed-meshheading:11877432-Open Reading Frames,
pubmed-meshheading:11877432-Repressor Proteins,
pubmed-meshheading:11877432-Sequence Homology, Amino Acid,
pubmed-meshheading:11877432-Thermotoga maritima,
pubmed-meshheading:11877432-Transcription Factors
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pubmed:year |
2002
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pubmed:articleTitle |
Crystal structure of Thermotoga maritima 0065, a member of the IclR transcriptional factor family.
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pubmed:affiliation |
Biosciences Division and Structural Biology Center, Argonne National Laboratory, Argonne, Illinois 60439, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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