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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5311
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pubmed:dateCreated |
1997-5-2
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pubmed:databankReference |
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pubmed:abstractText |
The crystal structure of the arabinose-binding and dimerization domain of the Escherchia coli gene regulatory protein AraC was determined in the presence and absence of L-arabinose. The 1.5 angstrom structure of the arabinose-bound molecule shows that the protein adopts an unusual fold, binding sugar within a beta barrel and completely burying the arabinose with the amino-terminal arm of the protein. Dimer contacts in the presence of arabinose are mediated by an antiparallel coiled-coil. In the 2.8 angstrom structure of the uncomplexed protein, the amino-terminal arm is disordered, uncovering the sugar-binding pocket and allowing it to serve as an oligomerization interface. The ligand-gated oligomerization as seen in AraC provides the basis of a plausible mechanism for modulating the protein's DNA-looping properties.
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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 |
Apr
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
421-5
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9103202-AraC Transcription Factor,
pubmed-meshheading:9103202-Arabinose,
pubmed-meshheading:9103202-Bacterial Proteins,
pubmed-meshheading:9103202-Binding Sites,
pubmed-meshheading:9103202-Crystallization,
pubmed-meshheading:9103202-Crystallography, X-Ray,
pubmed-meshheading:9103202-DNA,
pubmed-meshheading:9103202-Dimerization,
pubmed-meshheading:9103202-Hydrogen Bonding,
pubmed-meshheading:9103202-Ligands,
pubmed-meshheading:9103202-Models, Molecular,
pubmed-meshheading:9103202-Protein Conformation,
pubmed-meshheading:9103202-Protein Folding,
pubmed-meshheading:9103202-Protein Structure, Secondary,
pubmed-meshheading:9103202-Repressor Proteins,
pubmed-meshheading:9103202-Transcription Factors
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pubmed:year |
1997
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pubmed:articleTitle |
Structural basis for ligand-regulated oligomerization of AraC.
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pubmed:affiliation |
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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