 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](hv5159fig2mag.jpg)
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Figure 2
Overall and active-site structures of TtHGPRTase–IMP. (a) View of the dimer perpendicular to the molecular twofold axis. IMP (yellow) is represented by a ball-and-stick model. The hood and core domains of one subunit are represented by secondary structures in red and green, respectively. The other subunit is shown in dark grey. (b) Stereoview of the subunit structure showing secondary-structure assignments. α-Helices (green) are denoted a1–a4 and β-strands (yellow) are denoted b1–b7. The hood domain is shown in deep blue. IMP (purple) is represented by ball-and-stick model. (c) Superimposition of the Cα atoms of unliganded TtHGPRTase on those of TtHGPRTase–IMP. The unliganded and complexed forms are drawn in green and salmon, respectively. IMP (pink) is represented as a stick model. The residues shown as stick models show significant movement on binding IMP. (d) Stereoview of the active site. IMP and active-site residues are represented by ball-and-stick and stick models, respectively. Hydrogen bonds are shown as dotted lines. Water molecules (W1–W4) shown by orange circles occupy the binding site of PRPP pyrophosphate. Tyr155, which stacks on the 6-oxopurine ring of IMP, is omitted for clarity. The OMIT electron-density map contoured at the 1.0σ level was calculated using data to 1.89 Å resolution. |
![[Figure 2]](hv5159fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
