Metal ion chaperone function of the soluble Cu(I) receptor Atx1 - PubMed (original) (raw)
Metal ion chaperone function of the soluble Cu(I) receptor Atx1
R A Pufahl et al. Science. 1997.
Abstract
Reactive and potentially toxic cofactors such as copper ions are imported into eukaryotic cells and incorporated into target proteins by unknown mechanisms. Atx1, a prototypical copper chaperone protein from yeast, has now been shown to act as a soluble cytoplasmic copper(I) receptor that can adopt either a two- or three-coordinate metal center in the active site. Atx1 also associated directly with the Atx1-like cytosolic domains of Ccc2, a vesicular protein defined in genetic studies as a member of the copper-trafficking pathway. The unusual structure and dynamics of Atx1 suggest a copper exchange function for this protein and related domains in the Menkes and Wilson disease proteins.
Comment in
- Delivering copper inside yeast and human cells.
Valentine JS, Gralla EB. Valentine JS, et al. Science. 1997 Oct 31;278(5339):817-8. doi: 10.1126/science.278.5339.817. Science. 1997. PMID: 9381192 No abstract available.
Similar articles
- Cd2+- or Hg2+-binding proteins can replace the Cu+-chaperone Atx1 in delivering Cu+ to the secretory pathway in yeast.
Morin I, Cuillel M, Lowe J, Crouzy S, Guillain F, Mintz E. Morin I, et al. FEBS Lett. 2005 Feb 14;579(5):1117-23. doi: 10.1016/j.febslet.2005.01.008. FEBS Lett. 2005. PMID: 15710399 - Energetics of copper trafficking between the Atx1 metallochaperone and the intracellular copper transporter, Ccc2.
Huffman DL, O'Halloran TV. Huffman DL, et al. J Biol Chem. 2000 Jun 23;275(25):18611-4. doi: 10.1074/jbc.C000172200. J Biol Chem. 2000. PMID: 10764731 - Crystal structure of the Atx1 metallochaperone protein at 1.02 A resolution.
Rosenzweig AC, Huffman DL, Hou MY, Wernimont AK, Pufahl RA, O'Halloran TV. Rosenzweig AC, et al. Structure. 1999 Jun 15;7(6):605-17. doi: 10.1016/s0969-2126(99)80082-3. Structure. 1999. PMID: 10404590 - Copper chaperones, intracellular copper trafficking proteins. Function, structure, and mechanism of action.
Markossian KA, Kurganov BI. Markossian KA, et al. Biochemistry (Mosc). 2003 Aug;68(8):827-37. doi: 10.1023/a:1025740228888. Biochemistry (Mosc). 2003. PMID: 12948382 Review. - Atx1-like chaperones and their cognate P-type ATPases: copper-binding and transfer.
Singleton C, Le Brun NE. Singleton C, et al. Biometals. 2007 Jun;20(3-4):275-89. doi: 10.1007/s10534-006-9068-1. Epub 2007 Jan 16. Biometals. 2007. PMID: 17225061 Review.
Cited by
- Toward a molecular understanding of metal transport by P(1B)-type ATPases.
Rosenzweig AC, Argüello JM. Rosenzweig AC, et al. Curr Top Membr. 2012;69:113-36. doi: 10.1016/B978-0-12-394390-3.00005-7. Curr Top Membr. 2012. PMID: 23046649 Free PMC article. - N-Acetylcysteine interacts with copper to generate hydrogen peroxide and selectively induce cancer cell death.
Zheng J, Lou JR, Zhang XX, Benbrook DM, Hanigan MH, Lind SE, Ding WQ. Zheng J, et al. Cancer Lett. 2010 Dec 8;298(2):186-94. doi: 10.1016/j.canlet.2010.07.003. Epub 2010 Jul 27. Cancer Lett. 2010. PMID: 20667650 Free PMC article. - Identification of a novel zinc-binding protein, C1orf123, as an interactor with a heavy metal-associated domain.
Furukawa Y, Lim C, Tosha T, Yoshida K, Hagai T, Akiyama S, Watanabe S, Nakagome K, Shiro Y. Furukawa Y, et al. PLoS One. 2018 Sep 27;13(9):e0204355. doi: 10.1371/journal.pone.0204355. eCollection 2018. PLoS One. 2018. PMID: 30260988 Free PMC article. - Effect of prolonged incubation with copper on endothelium-dependent relaxation in rat isolated aorta.
Chiarugi A, Pitari GM, Costa R, Ferrante M, Villari L, Amico-Roxas M, Godfraind T, Bianchi A, Salomone S. Chiarugi A, et al. Br J Pharmacol. 2002 Aug;136(8):1185-93. doi: 10.1038/sj.bjp.0704816. Br J Pharmacol. 2002. PMID: 12163352 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases