Journalartikel

Jahr der Veröffentlichung: 2014

Seiten: 91-100

Zeitschrift: Acta Crystallographica. Section D: Biological Crystallography

Bandnummer: 70

Heftnummer: Part 1

ISSN: 0907-4449

eISSN: 1399-0047

Open Access Status: Bronze

DOI Link: https://doi.org/10.1107/S1399004713025285

Verlag: Wiley

Abstract: 
Glutaredoxins (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.

Harvard-Zitierstil: Yogavel, M., Tripathi, T., Gupta, A., Banday, M., Rahlfs, S., Becker, K., et al. (2014) Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins, Acta Crystallographica. Section D: Biological Crystallography, 70(Part 1), pp. 91-100. https://doi.org/10.1107/S1399004713025285

APA-Zitierstil: Yogavel, M., Tripathi, T., Gupta, A., Banday, M., Rahlfs, S., Becker, K., Belrhali, H., & Sharma, A. (2014). Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins. Acta Crystallographica. Section D: Biological Crystallography. 70(Part 1), 91-100. https://doi.org/10.1107/S1399004713025285