Fet3p is a multicopper oxidase (MCO)2 found in Saccharomyces cerevisiae with a structure consisting of three cupredoxin-like β-barrel domains and four copper ions located in three distinct metal sites (T1 in domain 3, T2, and the binuclear T3 at the interface between domains 1 and 3).[1][2] Fet3p is a type I membrane protein with an orientation that places the amino-terminal oxidase domain in the exocellular space (Nexo) and the carboxyl terminus in the cytoplasm (Ccyt).
Part of the ferroxidase reaction, Fet3p catalyzes the oxidation of Fe(II) to Fe(III) using O2 as substrate. The Fe(III) generated by Fet3p is a ligand for the iron permease, Ftr1p.
References
edit- ^ Sedlak, E.; Ziegler, L.; Kosman, D. J.; Wittung-Stafshede, P. (25 November 2008). "In vitro unfolding of yeast multicopper oxidase Fet3p variants reveals unique role of each metal site". Proceedings of the National Academy of Sciences. 105 (49): 19258–19263. Bibcode:2008PNAS..10519258S. doi:10.1073/pnas.0806431105. PMC 2614749. PMID 19033465.
- ^ Singh, A. (1 March 2006). "Assembly, Activation, and Trafficking of the Fet3p·Ftr1p High Affinity Iron Permease Complex in Saccharomyces cerevisiae". Journal of Biological Chemistry. 281 (19): 13355–13364. doi:10.1074/jbc.M512042200. PMID 16522632.
