Fig. 6: Intrinsic Euler angles describing the cap and core interdomain relationship for selected βPGM crystal structures with respect to the cis-P βPGMWT:MgF3:G6P complex. | Communications Biology

Fig. 6: Intrinsic Euler angles describing the cap and core interdomain relationship for selected βPGM crystal structures with respect to the cis-P βPGMWT:MgF3:G6P complex.

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

Fig. 6

a Roll angle (cap and core twisting motion) and pitch angle (cap and core closing angle). b Yaw angle (cap and core left-to-right lateral rotation) and pitch angle (cap and core closing angle). The βPGM species compared are: Open conformation: substrate-free cis-P βPGMWT (large black circles, PDB 2WHE26, small black circles, PDB 1ZOL21). NAC I conformation: cis-P βPGMWT:BeF3:G6P complex (gold circles, PDB 2WF927), cis-P βPGMD10N:F16BP complex (gold squares, PDB 8Q1D) and trans-A βPGMD10N,P146A:F16BP:MgT complex (gold diamonds, PDB 8Q1E). NAC III conformation: cis-P βPGMD10N:βG16BP complex (pink circles, PDB 5OK129), trans-A βPGMD10N,P146A:βG16BP:MgT complex (pink squares, PDB 8Q1F chain A) and trans-A βPGMD10N,P146A:βG16BP:MgT complex (pink diamonds, PDB 8Q1F chain B). Both chains of the trans-A βPGMD10N,P146A:βG16BP:MgT complex crystal structure are denoted as NAC IIIt conformations. Fully closed near-transition state conformation: cis-P βPGMWT:MgF3:G6P complex (large blue circles, PDB 2WF526) and cis-A βPGMP146A:MgF3:G6P complex (small blue circles. PDB 6YDJ13).

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