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. Author manuscript; available in PMC: 2012 Aug 5.
Published in final edited form as: J Mol Biol. 2011 May 31;411(1):190–200. doi: 10.1016/j.jmb.2011.05.036

Fig. 2.

Fig. 2

Structural changes of the α-carbon backbone associated with the binding of CP and PALA. (a,b) Structure of one catalytic chain of B. subtilis ATCase along with the 70s loop from the adjacent chain (70s loop*), and (c,d) one catalytic chain of E. coli ATCase along with the 80s loop from the adjacent chain (80s loop*) (a,c). The structure of the unliganded enzyme is shown with blue highlights, while the structure of the ATCase•CP complex is shown with red highlights, CP represented as spheres, and active site residues as sticks. (b,d) The structure of the ATCase•CP complex is shown with blue highlights, while the structure of the ATCase•PALA complex is shown with red highlights, PALA represented as spheres, and active site residues as sticks. The color spectral change from blue to red corresponds to 30 structures calculated linearly between the two determined X-ray structures. PDB entries 1ZA1,11 1ZA2,11 and 1D0925 were used for (c) and (d).