Crystallization and preliminary X-ray diffraction of malate dehydrogenase from Plasmodium falciparum.
The expression, purification, crystallization and preliminary X-ray diffraction characterization of malate dehydrogenase (MDH) from the malarial parasite Plasmodium falciparum (PfMDH) are reported. In order to gain a deeper understanding of the function and role of PfMDH, the protein was purified to homogeneity. The purified protein crystallized in space group P1, with unit-cell parameters a = 72, b = 157, c = 159 Å, α = 105, β = 101, γ = 95°. The resulting crystals diffracted to a maximal resolution of 2.24 Å and the structure has been solved by molecular replacement, with 16 monomers in the asymmetric unit. The 16 monomers are arranged into four independent tetramers, in agreement with previous reports demonstrating the tetrameric solution state of PfMDH. The X-ray structure of PfMDH is expected to clarify the differences in catalysis by PfMDH compared with other MDH family members and to provide a basis for the structure-based design of specific PfMDH inhibitors as well as general MDH inhibitors.
Department of Parasitology, Institute of Biomedical Science, University of São Paulo, Avenida Professor Lineu Prestes 1374, 05508-000 Sao Paulo, SP, Brazil.
Carsten
C
Wrenger
Ingrid B
IB
Müller
Sabine
S
Butzloff
Rositsa
R
Jordanova
Sergey
S
Lunev
Matthew R
MR
Groves
D003460:Crystallization; D018360:Crystallography, X-Ray; D008291:Malate Dehydrogenase / Q000737:chemistry*; D010963:Plasmodium falciparum / Q000201:enzymology*
D008291:Malate Dehydrogenase