Supplementary Materials

Supplementary Materials for:

An Intramolecular Switch Regulates Phosphoindependent FHA Domain Interactions in Mycobacterium tuberculosis

Timothy J. Nott, Geoff Kelly, Lasse Stach, Jiejin Li, Sarah Westcott, Dony Patel, Debbie M. Hunt, Steven Howell, Roger S. Buxton, Helen M. O�Hare, Stephen J. Smerdon

*To whom correspondence should be addressed. E-mail: stephen.smerdon{at}

This PDF file includes:

  • Methods
  • Fig. S1. Identification of binding partners of Rv1827.
  • Fig. S2. Rv1827 binds to phosphopeptides derived from its own N-terminal region.
  • Fig. S3. Biophysical analysis of full-length Rv1827 and Rv1827-pThr22.
  • Fig. S4. Comparison of the structures of Rv1827-pThr22 and the Chk2 FHA-phosphopeptide complex.
  • Fig. S5. The 1H-15N heteronuclear NOE and T1 relaxation profiles for Rv1827 and Rv1827-pThr22.
  • Fig. S6. Regulatory interactions of Rv1827 with KGD, GDH, and GS.
  • Table S1. NMR refinement statistics for Rv1827-pThr22.
  • Table S2. Comparison of ITC-derived binding parameters for full-length Rv1827 and the isolated FHA domain when titrated against pThr21- and pThr22-containing phosphopeptides.

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Citation: T. J. Nott, G. Kelly, L. Stach, J. Li, S. Westcott, D. Patel, D. M. Hunt, S. Howell, R. S. Buxton, H. M. O�Hare, S. J. Smerdon, An intramolecular switch regulates phosphoindependent FHA domain interactions in Mycobacterium tuberculosis. Sci. Signal.2, ra12 (2009).

© 2009 American Association for the Advancement of Science