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

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 cl...

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Bibliographic Details
Published in:Protein engineering 1999-11, Vol.12 (11), p.895-897
Main Authors: di Patti, Maria Carmela Bonaccorsi, Pascarella, Stefano, Catalucci, Daniele, Calabrese, Lilia
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Ascorbate Oxidase - chemistry
Azurin - analogs & derivatives
Azurin - chemistry
Binding Sites
Biological Transport
Carrier Proteins - metabolism
Ceruloplasmin - chemistry
Ceruloplasmin - metabolism
cupredoxin
ferroxidase activity
Fet3
Fungal Proteins - chemistry
homology modeling
Iron - metabolism
Membrane Transport Proteins - metabolism
Models, Molecular
Molecular Sequence Data
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Sequence Alignment
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Summary: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.
ISSN:0269-2139
1741-0126
1460-213X
1741-0134
DOI:10.1093/protein/12.11.895