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The structure of the transcriptional antiterminator NusB from Escherichia coli

  1. Author:
    Altieri, A. S.
    Mazzulla, M. J.
    Horita, D. A.
    Coats, R. H.
    Wingfield, P. T.
    Das, A.
    Court, D. L.
    Byrd, R. A.

  2. Author Address

    Byrd RA NCI, Frederick Canc Res & Dev Ctr, Struct Biophys Lab POB B,Bldg 538 Frederick, MD 21702 USA NCI, Frederick Canc Res & Dev Ctr, Struct Biophys Lab Frederick, MD 21702 USA NIAMSD, Prot Express Lab, NIH Bethesda, MD 20892 USA Univ Connecticut, Ctr Hlth, Dept Microbiol Farmington, CT 06030 USA NCI, Frederick Canc Res & Dev Ctr, Gene Regulat & Chromosome Biol Lab Frederick, MD 21702 USA
    1. Year: 2000
  2. Journal: Nature Structural Biology
    1. 7
    2. 6
    3. Pages: 470-474
  4. Type of Article: Article
  1. Abstract:

    We have determined the solution structure of NusB, a transcription antitermination protein from Escherichia coil, The structure reveals a novel, all a-helical protein fold. NusB mutations that cause a loss of function (NusB5) or alter specificity for RNA targets (NusB101) are localized to surface residues and likely affect RNA-protein or protein-protein interactions. Residues that are highly conserved among homologs stabilize the protein core. The solution structure of E. coliNusB presented here resembles that of Mycobacterium tuberculosis NusB determined by X-ray diffraction, but differs substantially from a solution structure of E. coil NusB reported earlier. [References: 38]

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