4HJM

Crystal structure of Glutaredoxin 1 from Plasmodium falciparum (PfGrx1) solved by S-SAD

Summary for 4HJM

• Entry DOI: 10.2210/pdb4hjm/pdb
• Related: 1KTE 3C1R
• Descriptor: Glutaredoxin, 3[N-MORPHOLINO]PROPANE SULFONIC ACID, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• Functional Keywords: glutathione, sulfur-sad, active site, plasticity, trx fold, redox enzymes, oxidoreductase
• Biological source: Plasmodium falciparum
• Total number of polymer chains: 1
• Total formula weight: 12763.89

Authors

Manickam, Y.,Sharma, A. (deposition date: 2012-10-13, release date: 2013-12-25, Last modification date: 2024-10-16)

Primary citation

Yogavel, M.,Tripathi, T.,Gupta, A.,Banday, M.M.,Rahlfs, S.,Becker, K.,Belrhali, H.,Sharma, A.
Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins.
Acta Crystallogr.,Sect.D, 70:91-100, 2014

PubMed 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.

PubMed: 24419382
DOI: 10.1107/S1399004713025285

Experimental method

X-RAY DIFFRACTION (1.5462 Å)