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. 2012 Dec;22(12):1716-20.
doi: 10.1038/cr.2012.156. Epub 2012 Nov 13.

Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region

Haishan Gao, Xiaojing Wu, Jijie Chai, Zhifu Han

Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region

Haishan Gao et al. Cell Res. 2012 Dec.
No abstract available

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Figures

Figure 1
Figure 1
Crystal structure of the dTale2 (148-610). (A) Domain organization and repeat compositions of dTale2 protein. N, N terminus; T3SS, type III secretion signal (colored in light blue); NLS, colored in yellow; AD, colored in light green; C, C terminus. The CRD is colored in red. Numerals indicate the residue numbers at the boundaries of different subdivisions. (B) Overall structure of dTale2 (148-610) (shown as cartoon representation, colored in rainbow). The numbers indicate the repeats along the super-helix. (C) Overall structure of the dTale2 NTR (148-288) (shown as cartoon, colored in rainbow). (D) Structural comparison of the NTR (162-288, cyan) to the first four canonical repeats (residues 289-424) in the CRD (light yellow). (E) Electrostatic potential surface of the NTR (positive potential, blue; negative potential, red). (F) Gel shift assay analysis of the dTale2 protein. Both the NTR (148-288) and the intact dTale2 (148-610) protein, but not the CRD (267-610), exhibited obvious shifts in mobility after incubation with dTale2-specified dsDNA. (G-J) ITC analysis of dTale2 proteins binding to dsDNA. The curves in the lower panels are the best fit to a one-set-of-sites binding model. The derived dissociation constants Kd are indicated. (G) The CRD could not well bind to specified DNA1. (H) The NTR (148-288) binds to specified DNA1. (I) The dTale2 (148-610) binds to specific DNA1. (J) The dTale2 (230-610) binds to specific DNA2. (K) The putative amino acids (sticks) in the NTR involved in DNA binding. The NTR is shown as surface representation (transparency 40%).
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