Pantothenate synthetase

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spinqualitylabelsall models Pantothenate synthetase complex with pantoate, AMPPNP (stick model), 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 (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 active site is located at the C-terminal of the central parallel β sheet. 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].

3D structures of pantothenate synthetase

Updated on 15-June-2016

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. ↑ Wang S, Eisenberg D. Crystal structure of the pantothenate synthetase from Mycobacterium tuberculosis, snapshots of the enzyme in action. Biochemistry. 2006 Feb 14;45(6):1554-61. PMID:16460002 doi:10.1021/bi051873e
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