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11-FOLD SYMMETRY OF THE TRP RNA-BINDING ATTENUATION PROTEIN (TRAP) FROM BACILLUS-SUBTILIS DETERMINED BY X-RAY-ANALYSIS

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Publication details

JournalJournal of Molecular Biology
DatePublished - 18 Nov 1994
Issue number1
Volume244
Number of pages5
Pages (from-to)15
Original languageEnglish

Abstract

The trp RNA-binding attenuation protein (TRAP) of Bacillus subtilis has been crystallized and examined by crystallography using X-ray synchrotron radiation diffraction data. Crystals of TRAP complexed with L-tryptophan belong to space group C2 with a = 156.8 Angstrom, b = 114.05 Angstrom, c = 105.9 Angstrom, beta = 118.2 degrees. Crystals of a potential heavy-atom derivative of TRAP complexed with 5-bromo-L-tryptophan grow in the same space group with similar cell dimensions. X-ray data for the native crystals and for the derivative have been collected to 2.9 Angstrom and 2.2 Angstrom resolution, respectively. Peaks in the self-rotation function and in the Patterson synthesis could only be explained by two 11-subunit oligomers (each formed by an 11-fold axis of symmetry) in the asymmetric unit lying with the 11-fold rotation axes parallel to each other. The consequence is that the TRAP molecule has 11-fold symmetry and contains 11 subunits.

    Research areas

  • TRP ATTENUATION PROTEIN, RNA-BINDING PROTEIN, CRYSTALLIZATION, X-RAY ANALYSIS, TRANSCRIPTION ATTENUATION, OPERON, EXPRESSION, MTRB

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