1zpu
From Proteopedia
(New page: 200px<br /><applet load="1zpu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1zpu, resolution 2.80Å" /> '''Crystal Structure of...) |
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| - | [[Image:1zpu.gif|left|200px]]<br /><applet load="1zpu" size=" | + | [[Image:1zpu.gif|left|200px]]<br /><applet load="1zpu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1zpu, resolution 2.80Å" /> | caption="1zpu, resolution 2.80Å" /> | ||
'''Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import'''<br /> | '''Crystal Structure of Fet3p, a Multicopper Oxidase that Functions in Iron Import'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Fet3p is a multicopper-containing glycoprotein localized to the yeast | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1ZPU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NAG, NDG and CU1 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1ZPU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=NDG:'>NDG</scene> and <scene name='pdbligand=CU1:'>CU1</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZPU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Hart, P | + | [[Category: Hart, P J.]] |
| - | [[Category: Kosman, D | + | [[Category: Kosman, D J.]] |
| - | [[Category: Stoj, C | + | [[Category: Stoj, C S.]] |
| - | [[Category: Taylor, A | + | [[Category: Taylor, A B.]] |
[[Category: Ziegler, L.]] | [[Category: Ziegler, L.]] | ||
[[Category: CU1]] | [[Category: CU1]] | ||
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[[Category: multicopper oxidase]] | [[Category: multicopper oxidase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:55 2008'' |
Revision as of 14:17, 21 February 2008
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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.
About this Structure
1ZPU is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Full crystallographic information is available from OCA.
Reference
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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