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Sci. Signal., 24 January 2012
[DOI: 10.1126/scisignal.2002525]

Supplementary Materials for:

A Phosphorylated Pseudokinase Complex Controls Cell Wall Synthesis in Mycobacteria

Christine L. Gee, Kadamba G. Papavinasasundaram, Sloane R. Blair, Christina E. Baer, Arnold M. Falick, David S. King, Jennifer E. Griffin, Harene Venghatakrishnan, Andrew Zukauskas, Jun-Rong Wei, Rakesh K. Dhiman, Dean C. Crick, Eric J. Rubin, Christopher M. Sassetti,* Tom Alber*

*To whom correspondence should be addressed. E-mail: christopher.sassetti{at}umassmed.edu (C.M.S.); tom{at}ucxray.berkeley.edu (T.A.)

This PDF file includes:

  • Fig. S1. MviN and FhaA proteins are conserved in M. tuberculosis and M. smegmatis.
  • Fig. S2. The Mt-MviN pseudokinase lacks sequence motifs that characterize active STPKs.
  • Fig. S3. Conserved features of Mt-MviN pseudokinase domain.
  • Fig. S4. Multiple Mtb Ser-Thr protein kinases phosphorylate Mt-MviN.
  • Fig. S5. FhaA FHA domain binds tightly to the phosphorylated Mt-MviN pseudokinase.
  • Fig. S6. FhaA is localized to the septum and poles in M. smegmatis.
  • Fig. S7. FhaA depletion in M. smegmatis leads to the accumulation of nascent PG at the poles.
  • Fig. S8. Structural comparison of the Mt-MviN pseudokinase with eukaryotic pseudokinases.
  • Table S1. Data collection and refinement statistics for Mt-MviN pseudokinase structures.
  • Table S2. Affinities of FhaA variants for the phosphorylated Mt-MviN KHD681–963.
  • References

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Citation: C. L. Gee, K. G. Papavinasasundaram, S. R. Blair, C. E. Baer, A. M. Falick, D. S. King, J. E. Griffin, H. Venghatakrishnan, A. Zukauskas, J.-R. Wei, R. K. Dhiman, D. C. Crick, E. J. Rubin, C. M. Sassetti, T. Alber, A Phosphorylated Pseudokinase Complex Controls Cell Wall Synthesis in Mycobacteria. Sci. Signal. 5, ra7 (2012).

© 2012 American Association for the Advancement of Science


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