Structural highlights
FunctionPublication Abstract from PubMedGlutaredoxins (Grxs) are redox proteins that use glutathione ((gamma)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. Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.,Yogavel M, Tripathi T, Gupta A, Banday MM, Rahlfs S, Becker K, Belrhali H, Sharma A Acta Crystallogr D Biol Crystallogr. 2014 Jan;70(Pt 1):91-100. doi:, 10.1107/S1399004713025285. Epub 2013 Dec 24. PMID:24419382[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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