Fig. 5: A steric clash is introduced between F16BP and V47 on the transition from a NAC I conformation to a NAC III conformation. | Communications Biology

Fig. 5: A steric clash is introduced between F16BP and V47 on the transition from a NAC I conformation to a NAC III conformation.

From: Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase

Fig. 5

Active site details of (a) the NAC I conformation of the cis-P βPGMD10N:F16BP complex (PDB 8Q1D), (b) a model with F16BP replacing βG16BP within the NAC III conformation of the cis-P βPGMD10N:βG16BP complex (PDB 5OK129), (c) the NAC III conformation of the cis-P βPGMD10N:βG16BP complex (PDB 5OK129), (d) the NAC I conformation of the trans-A βPGMD10N,P146A:F16BP:MgT complex (PDB 8Q1E), (e) a model with F16BP replacing βG16BP within the NAC III conformation of the trans-A βPGMD10N,P146A:βG16BP:MgT complex (PDB 8Q1F chain B) and (f) the NAC III conformation of the trans-A βPGMD10N,P146A:βG16BP:MgT complex (PDB 8Q1F chain B). Selected residues (sticks), together with F16BP (dark green carbon atoms), βG16BP (teal carbon atoms), structural waters (red spheres), Mgcat (green sphere) and MgT (green sphere) are illustrated. Yellow dashes indicate hydrogen bonds and black dashes show metal ion coordination. Magenta dashes and labels (b, e) specify heavy atom distances that comprise steric clashes between the carbonyl group of V47 and both the axial 2-hydroxyl group and the equatorial 3-hydroxyl group of F16BP on adoption of a NAC III conformation. Such close proximity between F16BP and residues of the substrate specificity loop (V36–L53) impedes the transition from a NAC I conformation to a NAC III conformation. G46 is highly conserved across members of the haloacid dehalogenase superfamily33, where it serves to coordinate βG16BP in a NAC III conformation (c, f) but has positional variability in a NAC I conformation (a, d).

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