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Protein Engineering, Vol. 12, No. 11, 895-897, November 1999
© 1999 Oxford University Press

Short Communication

Homology modeling of the multicopper oxidase Fet3 gives new insights in the mechanism of iron transport in yeast

Maria Carmela Bonaccorsi di Patti1, Stefano Pascarella, Daniele Catalucci2 and Lilia Calabrese2

Dip. Scienze Biochimiche `A.Rossi-Fanelli' and Centro di Biologia Molecolare del CNR, Università di Roma `La Sapienza', P.le A. Moro 5, 00185 Roma, Italy and 2 Dip. Biologia, Terza Università di Roma, V.le Marconi 446, 00146 Roma, Italy

Fet3, the multicopper oxidase of yeast, oxidizes extracellular ferrous iron which is then transported into the cell through the permease Ftr1. A three-dimensional model structure of Fet3 has been derived by homology modeling. Fet3 consists of three cupredoxin domains joined by a trinuclear copper cluster which is connected to the blue copper site located in the third domain. Close to this site, which is the primary electron acceptor from the substrate, residues for a potential iron binding site could be identified. The surface disposition of negatively charged residues suggests that Fet3 can translocate Fe3+ to the permease Ftr1 through a pathway under electrostatic guidance.

Keywords: cupredoxin/ferroxidase activity/Fet3/homology modeling

1 To whom correspondence should be addressed


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