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![[Figure 4]](mn5067fig4mag.jpg)
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Figure 4
Comparison of topology and electrostatic properties. (a, b, c) Topology and connectivity diagrams for GBS_NucA (H148A) (a), EndA (H160A) (b) and Spd1 (c). (d, e, f) Ribbon diagrams, viewing the `front' face of the enzymes, with the substrate-binding loops shown in red. For EndA (H160A) (e), this region was modeled on that of NucA (H148A) in space group P63 and the correct EndA sequence was threaded onto this structure. For Spd1 (f), this region lacked significant structural homology to either NucA or EndA. Therefore, the conformation of this loop was generated de novo using SWISS-MODEL (for details, see Supporting Information; Arnold et al., 2006  ). (g–l) Electrostatic surface potentials for NucA (H148A), EndA (H160A) and Spd1. For each model, any incomplete side chains were rebuilt using preferred side-chain rotamers (Lovell et al., 2000) and the least favored of all alternate conformations were removed. Electrostatic surface potentials were calculated using the Adaptive Poisson-Boltzmann Solver tool in PyMOL (Baker et al., 2001) and range from −2kT e−1 (electronegative, red) to 22kT e−1 (electropositive, blue). Regions of neutral charge are shown in white. The location of the active site is highlighted by a dashed yellow circle. |
![[Figure 4]](mn5067fig4.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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