8q1c | pdb_00008q1c

Substrate-free D10N,P146A variant of beta-phosphoglucomutase from Lactococcus lactis

spinqualitylabelsall models 8q1c, resolution 1.68Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8q1c is a 2 chain structure with sequence from Lactococcus lactis subsp. lactis Il1403. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.679Å Ligands: EDO, MG, PO4, TRS Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0A7T4I1_LACLL Publication Abstract from PubMed Metabolic regulation occurs through precise control of enzyme activity. Allomorphy is a post-translational fine control mechanism where the catalytic rate is governed by a conformational switch that shifts the enzyme population between forms with different activities. beta-Phosphoglucomutase (betaPGM) uses allomorphy in the catalysis of isomerisation of beta-glucose 1-phosphate to glucose 6-phosphate via beta-glucose 1,6-bisphosphate. Herein, we describe structural and biophysical approaches to reveal its allomorphic regulatory mechanism. Binding of the full allomorphic activator beta-glucose 1,6-bisphosphate stimulates enzyme closure, progressing through NAC I and NAC III conformers. Prior to phosphoryl transfer, loops positioned on the cap and core domains are brought into close proximity, modulating the environment of a key proline residue. Hence accelerated isomerisation, likely via a twisted anti/C4-endo transition state, leads to the rapid predominance of active cis-P betaPGM. In contrast, binding of the partial allomorphic activator fructose 1,6-bisphosphate arrests betaPGM at a NAC I conformation and phosphoryl transfer to both cis-P betaPGM and trans-P betaPGM occurs slowly. Thus, allomorphy allows a rapid response to changes in food supply while not otherwise impacting substantially on levels of important metabolites. Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in beta-phosphoglucomutase.,Cruz-Navarrete FA, Baxter NJ, Flinders AJ, Buzoianu A, Cliff MJ, Baker PJ, Waltho JP Commun Biol. 2024 Jul 27;7(1):909. doi: 10.1038/s42003-024-06577-9. PMID:39068257 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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