journal menu
![[Figure 6]](ba5238fig6mag.jpg)
|
|
Figure 6
(a) Overall (left) and close-up (right) views of the structure of βhingeHis6.AP2 (PDB entry 4uqi ). The residues of the hinge resolved in the structure are shown in green as a stick representation. The AP2 core is depicted as a surface representation coloured as in Fig. 1 ![[link]](../../../../../../logos/arrows/d_arr.gif) . The residues of the buried hinge are indicated in the close-up view, with electron density shown as a mesh (2mFo − DFc map contoured at 0.34 e− Å−3). Also shown are the positions of the selenium sites found in the bowl for each of the methionine mutants indicated, showing good agreement with the positions of the corresponding wild-type residues that were mutated. (b, c) Views of the hinge-binding site in the locked (b) and open (c) conformational states; in the `open' state (c), the hinge residues from the `locked' state βhingeH6.AP2 structure are superposed onto the `open' structure and shown in grey. Adapted from Kelly et al. (2014). |
![[Figure 6]](ba5238fig6.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
access
