PDBsum entry 4mzc

Oxidoreductase

PDB id: 4mzc

Contents

Protein chain

106 a.a.

Ligands

MPO

MPD

Waters ×199

PDB id:

4mzc

Name:

Oxidoreductase

Title:

Atomic resolution structure of pfgrx1

Structure:

Glutaredoxin. Chain: a. Synonym: glutaredoxin 1. Engineered: yes

Source:

Plasmodium falciparum. Organism_taxid: 36329. Strain: 3d7. Gene: grx1, pfc0271c. Expressed in: escherichia coli. Expression_system_taxid: 1007065.

Resolution:

0.95Å R-factor: 0.104 R-free: 0.111

Authors:

M.Yogavel,A.Sharma

Key ref:

M.Yogavel et al. (2014). Atomic resolution crystal structure of glutaredoxin 1 from Plasmodium falciparum and comparison with other glutaredoxins. Acta Crystallogr D Biol Crystallogr, 70, 91. PubMed id: 24419382 DOI: 10.1107/S1399004713025285

Date:

30-Sep-13 Release date: 09-Oct-13

Supersedes:

4kjf

Protein chain

Q9NLB2  (Q9NLB2_PLAF7) -  Glutaredoxin-1 from Plasmodium falciparum (isolate 3D7)

Seq: 111 a.a.

Struc: 106 a.a.

Enzyme reactions

• Enzyme class: E.C.1.20.4.1 - arsenate reductase (glutathione/glutaredoxin).
• Reaction: [glutaredoxin]-dithiol + arsenate + glutathione + H⁺ = glutathionyl-S- S-[glutaredoxin] + arsenite + H2O
• Cofactor: Mo cation

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

reference

DOI no: 10.1107/S1399004713025285

Acta Crystallogr D Biol Crystallogr 70:91 (2014)

PubMed id: 24419382

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

M.Yogavel, T.Tripathi, A.Gupta, M.M.Banday, S.Rahlfs, K.Becker, H.Belrhali, A.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.