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4kp7
From Proteopedia
Contents |
Structure of Plasmodium IspC in complex with a beta-thia-isostere derivative of Fosmidomycin
Template:ABSTRACT PUBMED 24032981
Function
[DXR_PLAFX] Catalyzes the NADP-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP).[1]
About this Structure
4kp7 is a 2 chain structure with sequence from Plafx. Full crystallographic information is available from OCA.
Reference
- Kunfermann A, Lienau C, Illarionov B, Held J, Grawert T, Behrendt CT, Werner P, Hahn S, Eisenreich W, Riederer U, Mordmuller B, Bacher A, Fischer M, Groll M, Kurz T. IspC as target for antiinfective drug discovery: Synthesis, enantiomeric separation and structural biology of fosmidomycin thia-isosters. J Med Chem. 2013 Sep 13. PMID:24032981 doi:10.1021/jm4012559
- ↑ Jomaa H, Wiesner J, Sanderbrand S, Altincicek B, Weidemeyer C, Hintz M, Turbachova I, Eberl M, Zeidler J, Lichtenthaler HK, Soldati D, Beck E. Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science. 1999 Sep 3;285(5433):1573-6. PMID:10477522
Categories: 1-deoxy-D-xylulose-5-phosphate reductoisomerase | Plafx | Bacher, A. | Groll, M. | Kunfermann, A. | Apicoplast | Drug optimization | Dxp pathway | Malaria | Nadph binding | Non-covalent inhibition | Oxidoreductase-oxidoreductase inhibitor complex | Reductoisomerase | Rossmann fold | Tuberculosis
