 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 4]](kw5076fig4mag.jpg)
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Figure 4
F1 binds and stabilizes dCK in the open state. (a) dCK–F1–UDP (green ribbon, open state) is overlaid on dCK in complex with deoxycytidine (dC) and ADP (r.m.s.d. of 0.50 Å over 144 Cα atoms), which represents the closed state (blue ribbon; PDB entry 2no1 ). The left panel shows how the loop carrying Ser74 is affected upon phosphorylation. Glu74 (the phosphomimetic residue of the phosphorylated Ser74) is now in contact distance with Trp58. The enlargement on the right displays in detail how the Trp58 side chain reorients and makes a new interaction with Glu74. Black arrows indicate the major transitions required between the closed and open states. Distances are in Å. (b) Surface representation of dCK in complex with F1 and UDP (green color with F1 depicted as red spheres; representing the open state) and dCK in complex with dC and ADP (blue color; representing the closed state) in the same orientation. In the closed state, the nucleoside is occluded and cannot dissociate from the enzyme. The larger F1 would not fit in the closed enzyme state and must bind to the open state that allows it to protrude into the solvent. |
![[Figure 4]](kw5076fig4.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
