PDBsum entry 3ctf

Oxidoreductase

PDB id: 3ctf

Contents

Protein chain

108 a.a. *

Waters ×105

* Residue conservation analysis

PDB id:

3ctf

Name:

Oxidoreductase

Title:

Crystal structure of oxidized grx2

Structure:

Glutaredoxin-2. Chain: a. Synonym: thioltransferase, glutathione-dependent oxidoreductase 2. Engineered: yes

Source:

Saccharomyces cerevisiae. Baker's yeast. Organism_taxid: 4932. Strain: s288c. Gene: grx2, ttr, ttr1, ydr513w, d9719.17. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.10Å R-factor: 0.222 R-free: 0.250

Authors:

J.Yu,Y.B.Teng,C.Z.Zhou

Key ref:

W.F.Li et al. (2010). Structural basis for the different activities of yeast Grx1 and Grx2. Biochim Biophys Acta, 1804, 1542-1547. PubMed id: 20417731

Date:

14-Apr-08 Release date: 11-Nov-08

Protein chain

P17695  (GLRX2_YEAST) -  Glutaredoxin-2 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: 143 a.a.

Struc: 108 a.a.

Enzyme reactions

• Enzyme class 2: E.C.1.11.1.9 - glutathione peroxidase.
• Reaction: 2 glutathione + H2O2 = glutathione disulfide + 2 H2O
• Cofactor: Se(2+)
• Enzyme class 3: E.C.2.5.1.18 - glutathione transferase.
• Reaction: RX + glutathione = an S-substituted glutathione + a halide anion + H⁺

Note, where more than one E.C. class is given (as above), each may correspond to a different protein domain or, in the case of polyprotein precursors, to a different mature protein.

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

reference

Biochim Biophys Acta 1804:1542-1547 (2010)

PubMed id: 20417731

Structural basis for the different activities of yeast Grx1 and Grx2.

W.F.Li, J.Yu, X.X.Ma, Y.B.Teng, M.Luo, Y.J.Tang, C.Z.Zhou.

ABSTRACT

Yeast glutaredoxins Grx1 and Grx2 catalyze the reduction of both inter- and intra-molecular disulfide bonds using glutathione (GSH) as the electron donor. Although sharing the same dithiolic CPYC active site and a sequence identity of 64%, they have been proved to play different roles during oxidative stress and to possess different glutathione-disulfide reductase activities. To address the structural basis of these differences, we solved the crystal structures of Grx2 in oxidized and reduced forms, at 2.10 A and 1.50 A, respectively. With the Grx1 structures we previously reported, comparative structural analyses revealed that Grx1 and Grx2 share a similar GSH binding site, except for a single residue substitution from Asp89 in Grx1 to Ser123 in Grx2. Site-directed mutagenesis in combination with activity assays further proved this single residue variation is critical for the different activities of yeast Grx1 and Grx2.