Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins

Acta Crystallographica. Section D, Biological Crystallography
Manickam YogavelAmit Sharma

Abstract

Glutaredoxins (Grxs) are redox proteins that use glutathione ((γ)Glu-Cys-Gly; GSH) as a cofactor. Plasmodium falciparum has one classic dithiol (CXXC) glutaredoxin (glutaredoxin 1; PfGrx1) and three monothiol (CXXS) Grx-like proteins (GLPs), which have five residue insertions prior to the active-site Cys. Here, the crystal structure of PfGrx1 has been determined by the sulfur single-wavelength anomalous diffraction (S-SAD) method utilizing intrinsic protein and solvent S atoms. Several residues were modelled with alternate conformations, and an alternate position was refined for the active-site Cys29 owing to radiation damage. The GSH-binding site is occupied by water polygons and buffer molecules. Structural comparison of PfGrx1 with other Grxs and Grx-like proteins revealed that the GSH-binding motifs (CXXC/CXXS, TVP, CDD, Lys26 and Gln/Arg63) are structurally conserved. Both the monothiol and dithiol Grxs possess three conserved water molecules; two of these were located in the GSH-binding site. PfGrx1 has several polar and charged amino-acid substitutions that provide structurally important additional hydrogen bonds and salt bridges missing in other Grxs.

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Citations

May 7, 2015·Acta Crystallographica. Section D, Biological Crystallography·Manuela GorgelThomas Boesen
Feb 18, 2017·Molecules : a Journal of Synthetic Chemistry and Natural Product Chemistry·Alberto Guevara-FloresIrene Patricia Del Arenal
Oct 23, 2018·Journal of Agricultural and Food Chemistry·Xiaomei SunSong-Qing Hu
Dec 7, 2021·The Journal of Physical Chemistry. B·Galo E BalattiSebastian Fernandez-Alberti

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