11-fold symmetry of the trp RNA-binding attenuation protein (TRAP) from Bacillus subtilis determined by X-ray analysis

J Mol Biol. 1994 Nov 18;244(1):1-5. doi: 10.1006/jmbi.1994.1698.


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 A, b = 114.05 A, c = 105.9 A, 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 A and 2.2 A 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacillus subtilis / chemistry*
  • Bacillus subtilis / genetics
  • Bacterial Proteins / chemistry*
  • Bacterial Proteins / metabolism
  • Crystallography, X-Ray
  • Cyclotrons
  • Models, Chemical
  • Operon / genetics
  • Protein Conformation
  • RNA, Bacterial / metabolism
  • RNA, Messenger / metabolism
  • RNA-Binding Proteins / chemistry*
  • RNA-Binding Proteins / metabolism
  • Transcription Factors / chemistry*
  • Transcription Factors / metabolism
  • Tryptophan / analogs & derivatives
  • Tryptophan / chemistry


  • Bacterial Proteins
  • MtrB protein, Bacteria
  • RNA, Bacterial
  • RNA, Messenger
  • RNA-Binding Proteins
  • Transcription Factors
  • 5-bromotryptophan
  • Tryptophan