Pantothenate synthetase

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Pantothenate (vitamin B5) biosynthesis is essential for the virulence of ''Mycobacterium tuberculosis'' thus its blockage can be used as a potential drug target<ref>PMID:26486566</ref>.
Pantothenate (vitamin B5) biosynthesis is essential for the virulence of ''Mycobacterium tuberculosis'' thus its blockage can be used as a potential drug target<ref>PMID:26486566</ref>.
== Structural highlights ==
== Structural highlights ==
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PS <scene name='52/525165/Cv/2'>active site is located at the C-terminal of the central parallel β sheet</scene>. 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<ref>PMID:12717031</ref>. Water molecules shown as red spheres.
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PS <scene name='52/525165/Cv/7'>active site is located at the C-terminal of the central parallel β sheet</scene>. 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<ref>PMID:12717031</ref>. Water molecules are shown as red spheres.
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*<scene name='52/525165/Cv/3'>Pantoate binding site</scene> (chain A).
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*<scene name='52/525165/Cv/8'>Pantoate binding site</scene> (chain A).
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*<scene name='52/525165/Cv/6'>AMPPNP binding site</scene> (chain B).
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*<scene name='52/525165/Cv/9'>AMPPNP binding site</scene> (chain B).
</StructureSection>
</StructureSection>
==3D structures of pantothenate synthetase==
==3D structures of pantothenate synthetase==

Revision as of 12:27, 29 July 2019

Pantothenate synthetase complex with pantoate, AMPPNP, sulfate, Mg+2 ion (green), ethanol and glycerol (PDB entry 1n2e)

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3D structures of pantothenate synthetase

Updated on 29-July-2019

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

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