 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](gx5220fig2mag.jpg)
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Figure 2
The structure of TbAK. The views are all of the A chain, but there is essentially no difference between the four molecules in the asymmetric unit. (a) The unbiased maximum-likelihood difference map calculated with REFMAC5 output coefficients contoured at 3σ before the ligands were added to the model. The positive contour is in blue and the negative contour is in red. The protein chain is shown as a semi-transparent ribbon. (b) Worm representations of the fold of the open apo form (coral core subunit and red lid) superposed on the closed form (ice blue). The structures were superposed using SSM (Krissinel & Henrick, 2004  ) based on the core subunit. The adenosine and ADP ligands are shown as spheres. (c) Surface view of the A chain, in which the two adenines can be seen to be buried in deep pockets. (d) Superposition of the anion-hole region of the TbAK–adenosine–ADP complex (ice blue; the protein was co-crystallized with AMPPNP, which is presumed to have hydrolysed) reported here with those of TbAK–AP5A (PDB entry 3otx
, coral; Kuettel et al., 2011) and human AK in complex with two adenosines (PDB entry 1bx4
, lemon; Mathews et al., 1998). The structures were superposed using SSM based on the Cα atoms in chain A of both. The ligands are shown as cylinders, with the C and P atoms coloured according to chain for clarity. (e) Superposition of TbAK–adenosine–ADP with TbAK–AP5A (PDB entry 3otx
). The ribbon shows the TbAK–adenosine–ADP trace. The ligands are shown as cylinders coloured as in (d). This figure was made with CCP4mg (McNicholas et al., 2011). |
![[Figure 2]](gx5220fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
