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Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site.

Weichsel A, Kem M, Montfort WR
Protein Sci 19 1801-6 (2010)
Related entries: 1ert, 1eru, 1erv, 1erw, 2hsh, 2hxk, 2ifq, 2iiy, 3m9k

Cited: 20 times
EuropePMC logo PMID: 20662007

Abstract

Thioredoxins reduce disulfide bonds and other thiol modifications in all cells using a CXXC motif. Human thioredoxin 1 is unusual in that it codes for an additional three cysteines in its 105 amino acid sequence, each of which have been implicated in other reductive activities. Cys 62 and Cys 69 are buried in the protein interior and lie at either end of a short helix (helix 3), and yet can disulfide link under oxidizing conditions. Cys 62 is readily S-nitrosated, giving rise to a SNO modification, which is also buried. Here, we present two crystal structures of the C69S/C73S mutant protein under oxidizing (1.5 A) and reducing (1.1 A) conditions. In the oxidized structure, helix 3 is unraveled and displays a new conformation that is stabilized by a series of new hydrogen bonds and a disulfide link with Cys 62 in a neighboring molecule. The new conformation provides an explanation for how a completely buried residue can participate in SNO exchange reactions.

Articles - 3m9j mentioned but not cited (8)

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  4. Crystal structure of human thioredoxin revealing an unraveled helix and exposed S-nitrosation site. Weichsel A, Kem M, Montfort WR. Protein Sci 19 1801-1806 (2010)
  5. Blind prediction of protein B-factor and flexibility. Bramer D, Wei GW. J Chem Phys 149 134107 (2018)
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Reviews citing this publication (3)

  1. The thioredoxin/peroxiredoxin/sulfiredoxin system: current overview on its redox function in plants and regulation by reactive oxygen and nitrogen species. Sevilla F, Camejo D, Ortiz-Espín A, Calderón A, Lázaro JJ, Jiménez A. J Exp Bot 66 2945-2955 (2015)
  2. Reactivity of thioredoxin as a protein thiol-disulfide oxidoreductase. Cheng Z, Zhang J, Ballou DP, Williams CH. Chem Rev 111 5768-5783 (2011)
  3. Modulation of signaling mechanisms in the heart by thioredoxin 1. Nagarajan N, Oka S, Sadoshima J. Free Radic Biol Med 109 125-131 (2017)

Articles citing this publication (9)

  1. Site-specific and redox-controlled S-nitrosation of thioredoxin. Barglow KT, Knutson CG, Wishnok JS, Tannenbaum SR, Marletta MA. Proc Natl Acad Sci U S A 108 E600-6 (2011)
  2. Contribution of Fdh3 and Glr1 to Glutathione Redox State, Stress Adaptation and Virulence in Candida albicans. Tillmann AT, Strijbis K, Cameron G, Radmaneshfar E, Thiel M, Munro CA, MacCallum DM, Distel B, Gow NA, Brown AJ. PLoS One 10 e0126940 (2015)
  3. Binding sites and hydrophobic pockets in Human Thioredoxin 1 determined by normal mode analysis. Philot EA, Perahia D, Braz AS, Costa MG, Scott LP. J Struct Biol 184 293-300 (2013)
  4. Protective effect of placenta extracts against nitrite-induced oxidative stress in human erythrocytes. Rozanova S, Cherkashina Y, Repina S, Rozanova K, Nardid O. Cell Mol Biol Lett 17 240-248 (2012)
  5. Binding of phenothiazines into allosteric hydrophobic pocket of human thioredoxin 1. Philot EA, da Mata Lopes D, de Souza AT, Braz AS, Nantes IL, Rodrigues T, Perahia D, Miteva MA, Scott LP. Eur Biophys J 45 279-286 (2016)
  6. Crystallographic studies evidencing the high energy tolerance to disrupting the interface disulfide bond of thioredoxin 1 from white leg shrimp Litopenaeus vannamei. Campos-Acevedo AA, Rudiño-Piñera E. Molecules 19 21113-21126 (2014)
  7. Deciphering the Path of S-nitrosation of Human Thioredoxin: Evidence of an Internal NO Transfer and Implication for the Cellular Responses to NO. Almeida VS, Miller LL, Delia JPG, Magalhães AV, Caruso IP, Iqbal A, Almeida FCL. Antioxidants (Basel) 11 1236 (2022)
  8. Purification and characterization of Taenia crassiceps cysticerci thioredoxin: insight into thioredoxin-glutathione-reductase (TGR) substrate recognition. Martínez-González JJ, Guevara-Flores A, Rendón JL, Sosa-Peinado A, Del Arenal Mena IP. Parasitol Int 64 194-201 (2015)
  9. Structures of the reduced and oxidized state of the mutant D24A of yeast thioredoxin 1: insights into the mechanism for the closing of the water cavity. Iqbal A, Moraes AH, Valente AP, Almeida FCL. J Biomol NMR 63 417-423 (2015)


Related citations provided by authors (2)

  1. Buried S-nitrosocysteine revealed in crystal structures of human thioredoxin.. Weichsel A, Brailey JL, Montfort WR Biochemistry 46 1219-27 (2007)
  2. Crystal structures of reduced, oxidized, and mutated human thioredoxins: evidence for a regulatory homodimer.. Weichsel A, Gasdaska JR, Powis G, Montfort WR Structure 4 735-51 (1996)

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