Several biological processes regulate the activity of target proteins through changes in the redox state of thiol groups (S2 to SH2), where a hydrogen donor is linked to an intermediary disulphide protein. Such processes include the ferredoxin/thioredoxin system, the NADP/thioredoxin system, and the glutathione/glutaredoxin system [1]. Several of these disulphide proteins share a common structure, consisting of a three-layer alpha/beta/alpha core. Proteins that contain domains with a thioredoxin-like fold include:

• Arsenate reductase (ArsC) [2]
• Calsequestrin (contains three tandem repeats of this fold) [3]
• Circadian oscillation regulator KaiB [4]
• Disulphide bond isomerase DsbC and DsbG (C-terminal domain) [5, 6]
• Disulphide bond facilitator DsbA (contains an alpha-helical insertion) [7]
• Endoplasmic reticulum protein ERP29 (N-terminal domain) [8]
• Glutathione S-transferase (GST) (N-terminal domain) [9]
• Mitochondrial ribosomal protein L51/S25/CI-B8 domain (variable positions for Cys residues in active site) [10]
• Phosducin [11]
• Protein disulphide isomerase (PDI) (contains two tandem repeats of this fold) [12]
• Glutathione peroxidase-like enzymes [13]
• Selenoprotein W-related [14]
• SH3-binding glutamic acid-rich protein like (SH3BGR) (lacks both conserved Cys residues) [15]
• Spliceosomal protein U5-15Kd [16]
• Thioltransferases, including thioredoxin [17], glutaredoxon [18], hybrid peroxiredoxin hyPrx5 [19]
• Thioredoxin-like 2Fe-2S ferredoxin [20]

1. Redox regulation: a broadening horizon. Nat. Struct. Biol. 56, 187-220
2. Insights into the structure, solvation, and mechanism of ArsC arsenate reductase, a novel arsenic detoxification enzyme. J. Biol. Chem. 9, 1071-81
3. Crystal structure of calsequestrin from rabbit skeletal muscle sarcoplasmic reticulum. Protein Sci. 5, 476-83
4. Anabaena circadian clock proteins KaiA and KaiB reveal a potential common binding site to their partner KaiC. EMBO J. 23, 1688-98
5. Crystal structure of the protein disulfide bond isomerase, DsbC, from Escherichia coli. Nat. Struct. Biol. 7, 196-9
6. Crystal structures of the DsbG disulfide isomerase reveal an unstable disulfide. J. Biomol. NMR 101, 8876-81
7. Structural analysis of three His32 mutants of DsbA: support for an electrostatic role of His32 in DsbA stability. Protein Sci. 6, 1893-900
8. Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer. Structure 9, 457-71
9. Calorimetric and structural studies of the nitric oxide carrier S-nitrosoglutathione bound to human glutathione transferase P1-1. null 15, 1093-105
10. The oxidized subunit B8 from human complex I adopts a thioredoxin fold. Biochem. Biophys. Res. Commun. 12, 1645-54
11. Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. J. Mol. Biol. 87, 577-88
12. The structure in solution of the b domain of protein disulfide isomerase. Cell 13, 357-68
13. The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution. Eur. J. Biochem. 133, 51-69
14. NMR structures of the selenoproteins Sep15 and SelM reveal redox activity of a new thioredoxin-like family. Protein Sci. 281, 3536-43
15. Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution. Proc. Natl. Acad. Sci. U.S.A. 318, 470-6
16. Identification, characterization and crystal structure analysis of the human spliceosomal U5 snRNP-specific 15 kD protein. J. Mol. Biol. 294, 515-25
17. Crystal structure of thioredoxin from Escherichia coli at 1.68 A resolution. J. Biol. Chem. 212, 167-84
18. NMR structure of oxidized Escherichia coli glutaredoxin: comparison with reduced E. coli glutaredoxin and functionally related proteins. Structure 1, 310-21
19. The tetrameric structure of Haemophilus influenza hybrid Prx5 reveals interactions between electron donor and acceptor proteins. Structure 278, 10790-8
20. High resolution crystal structures of the wild type and Cys-55-->Ser and Cys-59-->Ser variants of the thioredoxin-like [2Fe-2S] ferredoxin from Aquifex aeolicus. J. Biol. Chem. 277, 34499-507

Several biological processes regulate the activity of target proteins through changes in the redo
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