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pubmed:abstractText |
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 Fe(3+) to the permease Ftr1 through a pathway under electrostatic guidance.
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pubmed:affiliation |
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 Dip. Biologia, Terza Università di Roma, V. le Marconi 446, 00146 Roma, Italy.
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