1zpu: Difference between revisions

Revision as of 15:09, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1zpu.png

Template:STRUCTURE 1zpu

Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron ImportCrystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import

Template:ABSTRACT PUBMED 16230618

About this StructureAbout this Structure

1ZPU is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

The copper-iron connection in biology: structure of the metallo-oxidase Fet3p., Taylor AB, Stoj CS, Ziegler L, Kosman DJ, Hart PJ, Proc Natl Acad Sci U S A. 2005 Oct 25;102(43):15459-64. Epub 2005 Oct 17. PMID:16230618

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import'''
+===Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import===
-==Overview==
+<!--
-Fet3p is a multicopper-containing glycoprotein localized to the yeast plasma membrane that catalyzes the oxidation of Fe(II) to Fe(III). This ferrous iron oxidation is coupled to the reduction of O(2) to H(2)O and is termed the ferroxidase reaction. Fet3p-produced Fe(III) is transferred to the permease Ftr1p for import into the cytosol. The posttranslational insertion of four copper ions into Fet3p is essential for its activity, thus linking copper and iron homeostasis. The mammalian ferroxidases ceruloplasmin and hephaestin are homologs of Fet3p. Loss of the Fe(II) oxidation catalyzed by these proteins results in a spectrum of pathological states, including death. Here, we present the structure of the Fet3p extracellular ferroxidase domain and compare it with that of human ceruloplasmin and other multicopper oxidases that are devoid of ferroxidase activity. The Fet3p structure delineates features that underlie the unique reactivity of this and homologous multicopper oxidases that support the essential trafficking of iron in diverse eukaryotic organisms. The findings are correlated with biochemical and physiological data to cross-validate the elements of Fet3p that define it as both a ferroxidase and cuprous oxidase.
+The line below this paragraph, {{ABSTRACT_PUBMED_16230618}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16230618 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16230618}}
 ==About this Structure==
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 [[Category: Iron transport]]
 [[Category: Multicopper oxidase]]
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