3gzd › Citations

Biochemical discrimination between selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase.

Collins R, Johansson AL, Karlberg T, Markova N, van den Berg S, Olesen K, Hammarström M, Flores A, Schüler H, Schiavone LH, Brzezinski P, Arnér ES, Högbom M
PLoS One 7 e30581 (2012)
Cited: 15 times
EuropePMC logo PMID: 22295093

Abstract

Selenium and sulfur are two closely related basic elements utilized in nature for a vast array of biochemical reactions. While toxic at higher concentrations, selenium is an essential trace element incorporated into selenoproteins as selenocysteine (Sec), the selenium analogue of cysteine (Cys). Sec lyases (SCLs) and Cys desulfurases (CDs) catalyze the removal of selenium or sulfur from Sec or Cys and generally act on both substrates. In contrast, human SCL (hSCL) is specific for Sec although the only difference between Sec and Cys is the identity of a single atom. The chemical basis of this selenium-over-sulfur discrimination is not understood. Here we describe the X-ray crystal structure of hSCL and identify Asp146 as the key residue that provides the Sec specificity. A D146K variant resulted in loss of Sec specificity and appearance of CD activity. A dynamic active site segment also provides the structural prerequisites for direct product delivery of selenide produced by Sec cleavage, thus avoiding release of reactive selenide species into the cell. We thus here define a molecular determinant for enzymatic specificity discrimination between a single selenium versus sulfur atom, elements with very similar chemical properties. Our findings thus provide molecular insights into a key level of control in human selenium and selenoprotein turnover and metabolism.

Articles - 3gzd mentioned but not cited (3)

  1. A machine learning-based chemoproteomic approach to identify drug targets and binding sites in complex proteomes. Piazza I, Beaton N, Bruderer R, Knobloch T, Barbisan C, Chandat L, Sudau A, Siepe I, Rinner O, de Souza N, Picotti P, Reiter L. Nat Commun 11 4200 (2020)
  2. Biochemical discrimination between selenium and sulfur 1: a single residue provides selenium specificity to human selenocysteine lyase. Collins R, Johansson AL, Karlberg T, Markova N, van den Berg S, Olesen K, Hammarström M, Flores A, Schüler H, Schiavone LH, Brzezinski P, Arnér ES, Högbom M. PLoS One 7 e30581 (2012)
  3. X-ray structures of Nfs2, the plastidial cysteine desulfurase from Arabidopsis thaliana. Roret T, Pégeot H, Couturier J, Mulliert G, Rouhier N, Didierjean C. Acta Crystallogr F Struct Biol Commun 70 1180-1185 (2014)


Reviews citing this publication (4)

  1. Selenoproteins: molecular pathways and physiological roles. Labunskyy VM, Hatfield DL, Gladyshev VN. Physiol Rev 94 739-777 (2014)
  2. The relationship between selenoprotein P and glucose metabolism in experimental studies. Mao J, Teng W. Nutrients 5 1937-1948 (2013)
  3. Selenocysteine β-Lyase: Biochemistry, Regulation and Physiological Role of the Selenocysteine Decomposition Enzyme. Seale LA. Antioxidants (Basel) 8 E357 (2019)
  4. The unique tRNASec and its role in selenocysteine biosynthesis. Serrão VHB, Silva IR, da Silva MTA, Scortecci JF, de Freitas Fernandes A, Thiemann OH. Amino Acids 50 1145-1167 (2018)

Articles citing this publication (8)

  1. Disruption of the selenocysteine lyase-mediated selenium recycling pathway leads to metabolic syndrome in mice. Seale LA, Hashimoto AC, Kurokawa S, Gilman CL, Seyedali A, Bellinger FP, Raman AV, Berry MJ. Mol Cell Biol 32 4141-4154 (2012)
  2. Structural changes during cysteine desulfurase CsdA and sulfur acceptor CsdE interactions provide insight into the trans-persulfuration. Kim S, Park S. J Biol Chem 288 27172-27180 (2013)
  3. Chemical characterisation and speciation of organic selenium in cultivated selenium-enriched Agaricus bisporus. Maseko T, Callahan DL, Dunshea FR, Doronila A, Kolev SD, Ng K. Food Chem 141 3681-3687 (2013)
  4. Chalcogen Bonds Involving Selenium in Protein Structures. Carugo O, Resnati G, Metrangolo P. ACS Chem Biol 16 1622-1627 (2021)
  5. Formation of a Ternary Complex for Selenocysteine Biosynthesis in Bacteria. Silva IR, Serrão VH, Manzine LR, Faim LM, da Silva MT, Makki R, Saidemberg DM, Cornélio ML, Palma MS, Thiemann OH. J Biol Chem 290 29178-29188 (2015)
  6. Computational identification of a new SelD-like family that may participate in sulfur metabolism in hyperthermophilic sulfur-reducing archaea. Li GP, Jiang L, Ni JZ, Liu Q, Zhang Y. BMC Genomics 15 908 (2014)
  7. Trypanosomatid selenophosphate synthetase structure, function and interaction with selenocysteine lyase. da Silva MTA, Silva IRE, Faim LM, Bellini NK, Pereira ML, Lima AL, de Jesus TCL, Costa FC, Watanabe TF, Pereira HD, Valentini SR, Zanelli CF, Borges JC, Dias MVB, da Cunha JPC, Mittra B, Andrews NW, Thiemann OH. PLoS Negl Trop Dis 14 e0008091 (2020)
  8. Exploring the selenium-over-sulfur substrate specificity and kinetics of a bacterial selenocysteine lyase. Johnstone MA, Nelson SJ, O'Leary C, Self WT. Biochimie 182 166-176 (2021)


Quick links