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PDBsum entry 4mzc
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Oxidoreductase
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PDB id
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4mzc
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References listed in PDB file
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Key reference
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Title
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Atomic resolution crystal structure of glutaredoxin 1 from plasmodium falciparum and comparison with other glutaredoxins.
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Authors
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M.Yogavel,
T.Tripathi,
A.Gupta,
M.M.Banday,
S.Rahlfs,
K.Becker,
H.Belrhali,
A.Sharma.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2014,
70,
91.
[DOI no: ]
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PubMed id
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Abstract
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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.
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