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Akansha Sharma

Jaipur
As seen in: The Journal of Biological Chemistry

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Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance

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By Manickam Yogavel, Joanne E. Nettleship, Akansha Sharma, Karl Harlos
| The Journal of Biological Chemistry Verified
The genomes of the malaria-causing Plasmodium parasites encode a protein fused of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase (HPPK) and dihydropteroate synthase (DHPS) domains that catalyze sequential reactions in the folate biosynthetic pathway. Whereas higher organisms derive folate from their diet and lack the enzymes for its synthesis, most eubacteria and a number of lower eukaryotes including malaria parasites synthesize tetrahydrofolate via DHPS.
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Structure of 6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase-dihydropteroate synthase from Plasmodium vivax sheds light on drug resistance

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By Manickam Yogavel, Akansha Sharma, Karl Harlos, Joanne E. Nettleship
| The Journal of Biological Chemistry Verified
Author contributions: M.Y. conceptualization; M.Y. and Amit Sharma formal analysis; M.Y. and Amit Sharma supervision; M.Y. and Amit Sharma funding acquisition; M.Y. investigation; M.Y. writing-review and editing; Amit Sharma data curation; M.Y. solved the structure of HPPK-DHPS.; J.E.N. and K.H. provided the recombinant clones and collected diffraction data.; Akansha Sharma performed expression, purification and crystallization using a construct screened and developed by Joanne E.
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