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Regulatory Features of the trp Operon and the Crystal Structure of the trp RNA-binding Attenuation Protein from Bacillus stearothermophilus

โœ Scribed by Xiao-ping Chen; Alfred A. Antson; Min Yang; Pan Li; Chris Baumann; Eleanor J. Dodson; G.Guy Dodson; Paul Gollnick


Book ID
115629382
Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
569 KB
Volume
289
Category
Article
ISSN
0022-2836

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The DNA-binding protein HU from Bacillus stearothermophilus (HUBst) is a dimer with a molecular weight of 195 kDa that is capable of bending DNA. An x-ray structure has been determined previously [Tanaka et al. 1984) Nature, vol. 310, pp. 376-381], but no structure could be established for a large p