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. Author manuscript; available in PMC: 2010 Dec 1.
Published in final edited form as: Curr Opin Struct Biol. 2009 Nov 14;19(6):650–657. doi: 10.1016/j.sbi.2009.10.017

Figure 5. Phosphorylation autoinhibits GarA.

Figure 5

A. Schematic model of Mtb GarA inhibition [8]. The FHA domain (orange) engages the N-terminal tail (red) phosphorylated on Thr21 (by PknG) or Thr22 (by PknB), stabilizing a conformation that blocks binding of the STPKs and target enzymes GDH, KGD and GS. The N-terminal tail adopts many conformations in the on state. B. Ribbon diagram of the average NMR structure of GarA [8] showing the N-terminal tail (red) occluding the enzyme-binding surface. Spheres show pThr22 (atom colors) and sites where mutations block binding of all three (blue) or two of the three (light blue) unphosphorylated target enzymes. C. Superposition of the average NMR structures of OdhI [41], the GarA homolog in C. glutamicum, unphosphorylated (cyan) and phosphorylated on Thr15 (blue). Folding of the N-terminal tail into the pThr binding site causes little change in the core FHA domain structure.