1zpu
|
Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import
OverviewOverview
Fet3p is a multicopper-containing glycoprotein localized to the yeast, plasma membrane that catalyzes the oxidation of Fe(II) to Fe(III). This, ferrous iron oxidation is coupled to the reduction of O(2) to H(2)O and is, termed the ferroxidase reaction. Fet3p-produced Fe(III) is transferred to, the permease Ftr1p for import into the cytosol. The posttranslational, insertion of four copper ions into Fet3p is essential for its activity, thus linking copper and iron homeostasis. The mammalian ferroxidases, ceruloplasmin and hephaestin are homologs of Fet3p. Loss of the Fe(II), oxidation catalyzed by these proteins results in a spectrum of, pathological states, including death. Here, we present the structure of, the Fet3p extracellular ferroxidase domain and compare it with that of, human ceruloplasmin and other multicopper oxidases that are devoid of, ferroxidase activity. The Fet3p structure delineates features that, underlie the unique reactivity of this and homologous multicopper oxidases, that support the essential trafficking of iron in diverse eukaryotic, organisms. The findings are correlated with biochemical and physiological, data to cross-validate the elements of Fet3p that define it as both a, ferroxidase and cuprous oxidase.
About this StructureAbout this Structure
1ZPU is a Single protein structure of sequence from Saccharomyces cerevisiae with NAG, NDG and CU1 as ligands. Full crystallographic information is available from OCA.
ReferenceReference
The copper-iron connection in biology: structure of the metallo-oxidase Fet3p., Taylor AB, Stoj CS, Ziegler L, Kosman DJ, Hart PJ, Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15459-64. Epub 2005 Oct 17. PMID:16230618
Page seeded by OCA on Wed Nov 21 07:35:43 2007