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![[Figure 4]](dw5179fig4mag.jpg)
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Figure 4
Conformational change of MapZ. (a) Superposition of c-di-GMP-bound MapZ with c-di-GMP-bound MapZ in complex with CheR1; the crystal structure of c-di-GMP-bound MapZ (in complex with CheR1, this study) is in magenta and the NMR structure of c-di-GMP-bound MapZ with lowest energy (PDB entry 2l74; Habazettl et al., 2011  ) is in green. The C- and N-termini of the two MapZ structures are annotated. The N-termini of both structures wrap around two intercalated c-di-GMP molecules, but with different orientations. It is clear that the C-terminal helix in our crystal structure of MapZ (in magenta) shrinks towards the β-barrel. (b) Superposition of the NMR structure of c-di-GMP-bound MapZ with the lowest energy (PDB entry 2l74) and apo MapZ (PDB entry 1ywu; Ramelot et al., 2007); the c-di-GMP-bound MapZ structure is in green and the apo MapZ is in blue. The c-di-GMP in the complex structure is not displayed. Both the N- and C-termini of MapZ undergo a significant shift in position upon the binding of c-di-GMP. The structural rearrangement of MapZ may favour CheR1 binding. (c) Key residues for c-di-GMP binding in the complex structure (this study). Residues of MapZ are shown in red and Arg197 of CheR1 is in cyan. (d) Key residues for c-di-GMP binding in the NMR structure of c-di-GMP-bound MapZ. Residues of MapZ are shown in green. C-di-GMP molecules in both structures are in grey. Note the orientation of Arg8 and the position of Arg197 from a symmetry mate which forms a stacking interaction with the guanine bases of c-di-GMP. |
![[Figure 4]](dw5179fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
