A fragment-based approach identifies an allosteric pocket that impacts malate dehydrogenase activity

Reyes Romero A, Lunev S, Popowicz G, Calderone V, Gentili M, Sattler M, Plewka J, Taube M, Kozak M, Holak T, Dömling A, Groves M
Communications Biology 4(1) (2021 Aug 10)

doi: 10.1038/s42003-021-02442-1

Submitted to SASBDB: 2021 Mar 25 Published in SASBDB: 2021 Aug 11

SASDLQ2 – PfMDH L-lactate dehydrogenase, apo Sample: L-lactate dehydrogenase tetramer, 141 kDa Plasmodium falciparum protein Buffer: 100 mM Na-phosphate buffer, 400 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Xenocs Xeuss 2.0 with MetalJet, Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University on 2019 Jul 3 RgGuinier 3.4 nm Dmax 10.5 nm VolumePorod 211 nm3

SASDLR2 – PfMDH L-lactate dehydrogenase bound to inhibitor 2a Sample: L-lactate dehydrogenase tetramer, 141 kDa Plasmodium falciparum protein Buffer: 100 mM Na-phosphate buffer, 400 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Xenocs Xeuss 2.0 with MetalJet, Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University on 2019 Jul 3 RgGuinier 3.4 nm Dmax 10.5 nm VolumePorod 244 nm3

SASDLS2 – PfMDH L-lactate dehydrogenase bound to inhibitor 6a Sample: L-lactate dehydrogenase tetramer, 141 kDa Plasmodium falciparum protein Buffer: 100 mM Na-phosphate buffer, 400 mM NaCl, pH: 7.4 Experiment: SAXS data collected at Xenocs Xeuss 2.0 with MetalJet, Department of Macromolecular Physics, Faculty of Physics, Adam Mickiewicz University on 2019 Jul 3 RgGuinier 3.6 nm Dmax 11.4 nm VolumePorod 223 nm3