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Metal substitution in transferrins: specific binding of cerium(IV) revealed by the crystal structure of cerium-substituted human lactoferrin.

Baker HM, Baker CJ, Smith CA, Baker EN
J Biol Inorg Chem 5 692-8 (2000)
Cited: 25 times
EuropePMC logo PMID: 11128996

Abstract

Proteins of the transferrin family play a key role in iron homeostasis through their extremely strong binding of iron, as Fe3+. They are nevertheless able to bind a surprisingly wide variety of other metal ions. To investigate how metal ions of different size, charge and coordination characteristics are accommodated, we have determined the crystal structure of human lactoferrin (Lf) complexed with Ce4+. The structure, refined at 2.2 A resolution (R=20.2%, Rfree=25.7%) shows that the two Ce4+ ions occupy essentially the same positions as do Fe3+, and that the overall protein structure is unchanged; the same closed structure is formed for Ce2Lf as for Fe2Lf. The larger metal ion is accommodated by small shifts in the protein ligands, made possible by the presence of water molecules adjacent to each binding site. The two Ce4+ sites are equally occupied, indicating that the known difference in the pH-dependent release of Ce4+ arises from a specific protonation event, possibly of the His ligand in one of the binding sites. Comparing the effects of binding Ce4+ with those for the binding of other metal ions, we conclude that the ability of transferrins to accommodate metal ions other than Fe3+ depends on an interplay of charge, size, coordination and geometrical preferences of the bound metal ion. However, it is the ability to accept the six-coordinate, approximately octahedral, site provided by the protein that is of greatest importance.

Reviews - 1fck mentioned but not cited (2)

  1. Lactoferrin a multiple bioactive protein: an overview. García-Montoya IA, Cendón TS, Arévalo-Gallegos S, Rascón-Cruz Q. Biochim Biophys Acta 1820 226-236 (2012)
  2. Immunomodulatory effects of lactoferrin. Siqueiros-Cendón T, Arévalo-Gallegos S, Iglesias-Figueroa BF, García-Montoya IA, Salazar-Martínez J, Rascón-Cruz Q. Acta Pharmacol. Sin. 35 557-566 (2014)

Articles - 1fck mentioned but not cited (5)

  1. Structure of a complex of human lactoferrin N-lobe with pneumococcal surface protein a provides insight into microbial defense mechanism. Senkovich O, Cook WJ, Mirza S, Hollingshead SK, Protasevich II, Briles DE, Chattopadhyay D. J. Mol. Biol. 370 701-713 (2007)
  2. Structure and domain dynamics of human lactoferrin in solution and the influence of Fe(III)-ion ligand binding. Sill C, Biehl R, Hoffmann B, Radulescu A, Appavou MS, Farago B, Merkel R, Richter D. BMC Biophys 9 7 (2016)
  3. Improving mass spectrometry analysis of protein structures with arginine-selective chemical cross-linkers. Jones AX, Cao Y, Tang YL, Wang JH, Ding YH, Tan H, Chen ZL, Fang RQ, Yin J, Chen RC, Zhu X, She Y, Huang N, Shao F, Ye K, Sun RX, He SM, Lei X, Dong MQ. Nat Commun 10 3911 (2019)
  4. Low molecular weight chitosan oligosaccharides form stable complexes with human lactoferrin. Li J, Guan S, Cai B, Li Q, Rong S. FEBS Open Bio 13 2215-2223 (2023)
  5. Regulation of Iron Homeostasis through Parkin-Mediated Lactoferrin Ubiquitylation. Gholkar AA, Schmollinger S, Velasquez EF, Lo YC, Cohn W, Capri J, Dharmarajan H, Deardorff WJ, Gao LW, Abdusamad M, Whitelegge JP, Torres JZ. Biochemistry 59 2916-2921 (2020)


Reviews citing this publication (4)

  1. Lactoferrin, a Pleiotropic Protein in Health and Disease. Mayeur S, Spahis S, Pouliot Y, Levy E. Antioxid. Redox Signal. 24 813-836 (2016)
  2. Unveiling molecular mechanisms of pneumococcal surface protein A interactions with antibodies and lactoferrin. Jedrzejas MJ. Clin. Chim. Acta 367 1-10 (2006)
  3. Lactoferrin: Structure, function, denaturation and digestion. Wang B, Timilsena YP, Blanch E, Adhikari B. Crit Rev Food Sci Nutr 59 580-596 (2019)
  4. Regulation of zinc-dependent enzymes by metal carrier proteins. Thompson MW. Biometals 35 187-213 (2022)

Articles citing this publication (14)

  1. An iron-dependent and transferrin-mediated cellular uptake pathway for plutonium. Jensen MP, Gorman-Lewis D, Aryal B, Paunesku T, Vogt S, Rickert PG, Seifert S, Lai B, Woloschak GE, Soderholm L. Nat. Chem. Biol. 7 560-565 (2011)
  2. Apolactoferrin inhibits the catalytic domain of matrix metalloproteinase-2 by zinc chelation. Newsome AL, Johnson JP, Seipelt RL, Thompson MW. Biochem. Cell Biol. 85 563-572 (2007)
  3. Sensitizing curium luminescence through an antenna protein to investigate biological actinide transport mechanisms. Sturzbecher-Hoehne M, Goujon C, Deblonde GJ, Mason AB, Abergel RJ. J. Am. Chem. Soc. 135 2676-2683 (2013)
  4. The role of transferrin in actinide(IV) uptake: comparison with iron(III). Jeanson A, Ferrand M, Funke H, Hennig C, Moisy P, Solari PL, Vidaud C, Den Auwer C. Chemistry 16 1378-1387 (2010)
  5. Effect of cerium lanthanide on Hela and MCF-7 cancer cell growth in the presence of transferring. Palizban AA, Sadeghi-Aliabadi H, Abdollahpour F. Res Pharm Sci 5 119-125 (2010)
  6. Positive selection drives lactoferrin evolution in mammals. Liang GM, Jiang XP. Genetica 138 757-762 (2010)
  7. "Anion clamp" allows flexible protein to impose coordination geometry on metal ions. Wang M, Lai TP, Wang L, Zhang H, Yang N, Sadler PJ, Sun H. Chem. Commun. (Camb.) 51 7867-7870 (2015)
  8. Biokinetics of Nanomaterials: the Role of Biopersistence. Laux P, Riebeling C, Booth AM, Brain JD, Brunner J, Cerrillo C, Creutzenberg O, Estrela-Lopis I, Gebel T, Johanson G, Jungnickel H, Kock H, Tentschert J, Tlili A, Schäffer A, Sips AJAM, Yokel RA, Luch A. NanoImpact 6 69-80 (2017)
  9. Structural biology of the lanthanides-mining rare earths in the Protein Data Bank. Djinovic-Carugo K, Carugo O. J. Inorg. Biochem. 143 69-76 (2015)
  10. Interfacial adsorption and denaturization of human milk and recombinant rice lactoferrin. Pan F, Zhao X, Waigh TA, Lu JR, Miano F. Biointerphases 3 FB36 (2008)
  11. Binding of ReO4(-) with an engineered MoO4(2-)-binding protein: towards a new approach in radiopharmaceutical applications. Aryal BP, Brugarolas P, He C. J. Biol. Inorg. Chem. 17 97-106 (2012)
  12. Neptunium uptake by serum transferrin. Llorens I, Den Auwer C, Moisy P, Ansoborlo E, Vidaud C, Funke H. FEBS J. 272 1739-1744 (2005)
  13. Adenocarcinoma cells isolated from patients in the presence of cerium and transferrin in vitro. Zende-Del A, Gholami MR, Abdollahpour F, Ahmadvand H. J Med Life 8 436-439 (2015)
  14. Bone Mineral Density in Population Long-Term Exposed to Rare Earth Elements from a Mining Area of China. Liu H, Liu H, Yang Z, Wang K. Biol Trace Elem Res 199 453-464 (2021)


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