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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 |
2006-5-29
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pubmed:databankReference |
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pubmed:abstractText |
The crystal structure of Escherichia coli PhnF C-terminal domain (C-PhnF) was solved at 1.7 A resolution by the single wavelength anomalous dispersion (SAD) method. The PhnF protein belongs to the HutC subfamily of the large GntR transcriptional regulator family. Members of this family share similar N-terminal DNA-binding domains, but are divided into four subfamilies according to their heterogenic C-terminal domains, which are involved in effector binding and oligomerization. The C-PhnF structure provides for the first time the scaffold of this domain for the HutC subfamily, which covers about 31% of GntR-like regulators. The structure represents a mixture of alpha-helices and beta-strands, with a six-stranded antiparallel beta-sheet at the core. C-PhnF monomers form a dimer by establishing interdomain eight-strand beta-sheets that include core antiparallel and N-terminal two-strand parallel beta-sheets from each monomer. C-PhnF shares strong structural similarity with the chorismate lyase fold, which features a buried active site locked behind two helix-turn-helix loops. The structural comparison of the C-PhnF and UbiC proteins allows us to propose that a similar site in the PhnF structure is adapted for effector binding.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-10089316,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-10331874,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-10473770,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-10734204,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-10944333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-11013219,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-11279025,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-11296236,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-11455603,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-11756427,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-11877432,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-12706730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-12757941,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-12824325,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-12897000,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-15299926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-15556475,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-15680762,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-1579569,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-15944459,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-2060763,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-2203753,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-2843515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-3170481,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-3413113,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-7805834,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-7961501,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-8107132,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-8366038,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-8388873,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-8755887,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16672238-9409145
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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/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/GntR protein, E coli,
http://linkedlifedata.com/resource/pubmed/chemical/HutC protein, Klebsiella aerogenes,
http://linkedlifedata.com/resource/pubmed/chemical/Oxo-Acid-Lyases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors,
http://linkedlifedata.com/resource/pubmed/chemical/chorismate pyruvate lyase
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0961-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
15
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1506-11
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16672238-Amino Acid Sequence,
pubmed-meshheading:16672238-Bacterial Proteins,
pubmed-meshheading:16672238-Binding Sites,
pubmed-meshheading:16672238-Crystallography, X-Ray,
pubmed-meshheading:16672238-DNA,
pubmed-meshheading:16672238-DNA-Binding Proteins,
pubmed-meshheading:16672238-Escherichia coli Proteins,
pubmed-meshheading:16672238-Models, Molecular,
pubmed-meshheading:16672238-Molecular Sequence Data,
pubmed-meshheading:16672238-Oxo-Acid-Lyases,
pubmed-meshheading:16672238-Protein Conformation,
pubmed-meshheading:16672238-Protein Structure, Tertiary,
pubmed-meshheading:16672238-Repressor Proteins,
pubmed-meshheading:16672238-Sequence Homology, Amino Acid,
pubmed-meshheading:16672238-Signal Transduction,
pubmed-meshheading:16672238-Structural Homology, Protein,
pubmed-meshheading:16672238-Transcription Factors
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pubmed:year |
2006
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pubmed:articleTitle |
Structural characterization of GntR/HutC family signaling domain.
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pubmed:affiliation |
Ontario Center for Structural Proteomics, University Health Network, University of Toronto, Toronto, Ontario M5G 1L7, Canada.
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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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