Fig. 4: Conformational variation in the active site of βPGM. | Communications Biology

Fig. 4: Conformational variation in the active site of βPGM.

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

Fig. 4

Active site details of (a) the cis-P βPGMD10N:F16BP complex (PDB 8Q1D), (b) the cis-P βPGMD10N:βG16BP complex (PDB 5OK129), (c) the trans-A βPGMD10N,P146A:F16BP:MgT complex (PDB 8Q1E) and (d) the trans-A βPGMD10N,P146A:βG16BP:MgT complex (PDB 8Q1F chain A). 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. Apart from R49, residues of the substrate specificity loop (V36–L53) have been omitted for clarity. For the complexes containing a cis K145-P146 peptide bond (a, b), the alkylammonium sidechain of K145 is engaged in the active site, whereas for the complexes containing a trans K145-A146 peptide (c, d), the alkylammonium sidechain occupies a solvent exposed position, with MgT acting as a weakly-binding surrogate for the missing cation.

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