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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5
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pubmed:dateCreated |
1999-6-3
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pubmed:databankReference |
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pubmed:abstractText |
The arginine repressor (ArgR) is a hexameric DNA-binding protein that plays a multifunctional role in the bacterial cell. Here, we present the 2.5 A structure of apo-ArgR from Bacillus stearothermophilus and the 2.2 A structure of the hexameric ArgR oligomerization domain with bound arginine. This first view of intact ArgR reveals an approximately 32-symmetric hexamer of identical subunits, with six DNA-binding domains surrounding a central oligomeric core. The difference in quaternary organization of subunits in the arginine-bound and apo forms provides a possible explanation for poor operator binding by apo-ArgR and for high affinity binding in the presence of arginine.
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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 |
1072-8368
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
427-32
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10331868-Amino Acid Sequence,
pubmed-meshheading:10331868-Arginine,
pubmed-meshheading:10331868-Bacterial Proteins,
pubmed-meshheading:10331868-Binding Sites,
pubmed-meshheading:10331868-Crystallization,
pubmed-meshheading:10331868-Crystallography, X-Ray,
pubmed-meshheading:10331868-DNA-Binding Proteins,
pubmed-meshheading:10331868-Geobacillus stearothermophilus,
pubmed-meshheading:10331868-Models, Molecular,
pubmed-meshheading:10331868-Molecular Sequence Data,
pubmed-meshheading:10331868-Operator Regions, Genetic,
pubmed-meshheading:10331868-Peptide Fragments,
pubmed-meshheading:10331868-Protein Binding,
pubmed-meshheading:10331868-Protein Conformation,
pubmed-meshheading:10331868-Recombinant Proteins,
pubmed-meshheading:10331868-Repressor Proteins,
pubmed-meshheading:10331868-Solvents
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pubmed:year |
1999
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pubmed:articleTitle |
Structure of the arginine repressor from Bacillus stearothermophilus.
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pubmed:affiliation |
Department of Biochemistry & Biophysics and Johnson Research Foundation, University of Pennsylvania School of Medicine, Philadelphia 19104, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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