ArticleProceedings of the National Academy of Sciences of the United States of America2008
In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- The Ferroxidase-Permease System for Transport of Iron Across Membranes: From Yeast to Humans.International journal of molecular sciences · 2025Review
- Bacterial-type ferroxidase tunes iron-dependent phosphate sensing during Arabidopsis root development.Current biology : CB · 2022Article
- Identification and analysis of iron transporters from the fission yeast Schizosaccharomyces pombe.Archives of microbiology · 2022Article
- Synergistic Effects of Copper Sites on Apparent Stability of Multicopper Oxidase, Fet3p.International journal of molecular sciences · 2018Article
- Activity-stability relationships revisited in blue oxidases catalyzing electron transfer at extreme temperatures.Extremophiles : life under extreme conditions · 2016Article
- The Tat Substrate CueO Is Transported in an Incomplete Folding State.The Journal of biological chemistry · 2016Article
- Potassium and the K+/H+ Exchanger Kha1p Promote Binding of Copper to ApoFet3p Multi-copper Ferroxidase.The Journal of biological chemistry · 2016Article
- Advanced analyses of kinetic stabilities of iggs modified by mutations and glycosylation.Protein science : a publication of the Protein Society · 2015Article
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- Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.European biophysics journal : EBJ · 2011Article
- Characterization of a dipartite iron uptake system from uropathogenic Escherichia coli strain F11.The Journal of biological chemistry · 2011Article
- The removal of a disulfide bridge in CotA-laccase changes the slower motion dynamics involved in copper binding but has no effect on the thermodynamic stability.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2011Article
- Core glycan in the yeast multicopper ferroxidase, Fet3p: a case study of N-linked glycosylation, protein maturation, and stability.Protein science : a publication of the Protein Society · 2010Article
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4 authors.
Funding
Abstract
Fet3p from Saccharomyces cerevisiae is a multicopper oxidase (MCO) that contains 3 cupredoxin-like beta-barrel domains and 4 copper ions located in 3 distinct metal sites (T1 in domain 3, T2, and the binuclear T3 at the interface between domains 1 and 3). To better understand how protein structure and stability is defined by cofactor coordination in MCO proteins, we assessed thermal unfolding of apo and metallated forms of Fet3p by using spectroscopic and calorimetric methods in vitro (pH 7). We find that unfolding reactions of apo and different holo forms of Fet3p are irreversible reactions that depend on the scan rate. The domains in apo-Fet3p unfold sequentially [thermal midpoint (T(m)) of 45 degrees C, 62 degrees C, and 72 degrees C; 1 K/min]. Addition of T3 imposes strain in the apo structure that results in coupled domain unfolding and low stability (T(m) of 50 degrees C; 1 K/min). Further inclusion of T2 (i.e., only T1 absent) increases overall stability by approximately 5 degrees C but unfolding remains coupled in 1 step. Introduction of T1, producing fully-loaded holo-Fet3p (or in the absence of T2), results in stabilization of domain 3, which uncouples unfolding of the domains; unfolding of domain 2 occurs first along with Cu-site perturbations (T(m) 50-55 degrees C; 1 K/min), followed by unfolding of domains 1 and 3 ( approximately 65-70 degrees C; 1 K/min). Our results suggest that there is a metal-induced tradeoff between overall protein stability and metal coordination in members of the MCO family.
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