Summary for 4MZC
| Entry DOI | 10.2210/pdb4mzc/pdb |
| Related | 1KTE 3C1R 3CTG 4HJM 4MZB |
| 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 enzyme, oxidoreductase |
| Biological source | Plasmodium falciparum |
| Total number of polymer chains | 1 |
| Total formula weight | 12763.89 |
| Authors | Yogavel, M.,Sharma, A. (deposition date: 2013-09-30, release date: 2013-10-09, Last modification date: 2024-11-27) |
| 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 Cited by 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: 24419382DOI: 10.1107/S1399004713025285 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.949 Å) |
Structure validation
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