Pantothenate synthetase

From Proteopedia

Current revision

spinqualitylabelsall models Pantothenate synthetase complex with pantoate, AMPPNP, sulfate, Mg+2 ion (green), ethanol and glycerol (PDB entry 1n2e) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Pantothenate synthetase or pantoate-beta-alanine ligase (PS) catalyzes the ATP-dependent condensation of pantoate and β-alanine to form pantothenate[1]. Relevance Pantothenate (vitamin B5) biosynthesis is essential for the virulence of Mycobacterium tuberculosis thus its blockage can be used as a potential drug target[2]. Structural highlights PS . In this structure the pantoate substrate electron density is well defined in one subunit while the nucleotide electron density is well defined in the other[3]. Water molecules are shown as red spheres. (chain A). (chain B).

3D structures of pantothenate synthetase

Updated on 21-August-2023

References

1. ↑ Jonczyk R, Ronconi S, Rychlik M, Genschel U. Pantothenate synthetase is essential but not limiting for pantothenate biosynthesis in Arabidopsis. Plant Mol Biol. 2008 Jan;66(1-2):1-14. Epub 2007 Oct 12. PMID:17932772 doi:http://dx.doi.org/10.1007/s11103-007-9248-6
2. ↑ Hung AW, Silvestre HL, Wen S, George GP, Boland J, Blundell TL, Ciulli A, Abell C. Optimization of Inhibitors of Mycobacterium tuberculosis Pantothenate Synthetase Based on Group Efficiency Analysis. ChemMedChem. 2016 Jan 5;11(1):38-42. doi: 10.1002/cmdc.201500414. Epub 2015 Oct, 21. PMID:26486566 doi:http://dx.doi.org/10.1002/cmdc.201500414
3. ↑ Wang S, Eisenberg D. Crystal structures of a pantothenate synthetase from M. tuberculosis and its complexes with substrates and a reaction intermediate. Protein Sci. 2003 May;12(5):1097-108. PMID:12717031