Fig. 2: βPGM enzyme architecture. | Communications Biology

Fig. 2: βPGM enzyme architecture.

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

Fig. 2

Cartoon representation of substrate-free cis-P βPGM (PDB 2WHE26) highlighting the architecture of the helical cap domain (T16–V87) and the α/β core domain (M1–D15 and S88–K221). The active site is located in the cleft formed between the domains and rotation at the hinge results in closure of the active site during catalysis. Key functional loops and structural motifs are indicated: general acid-base hinge (dark red, F7–E18), substrate specificity loop (teal, V36–L53), 80 s hinge (purple, N79–S88), phosphodianions bridging loop (green, A113–N118), allomorphic control loop (orange, E140–I150), Mgcat site (pink, E169–S171, V188) and 170 s α-helix (cyan, Q172–K179). The location of Mgcat is shown by a green sphere.

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