1rq1
From Proteopedia
(New page: 200px<br /><applet load="1rq1" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rq1, resolution 2.8Å" /> '''Structure of Ero1p, S...) |
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| - | [[Image:1rq1.jpg|left|200px]]<br /><applet load="1rq1" size=" | + | [[Image:1rq1.jpg|left|200px]]<br /><applet load="1rq1" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rq1, resolution 2.8Å" /> | caption="1rq1, resolution 2.8Å" /> | ||
'''Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell'''<br /> | '''Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The flavoenzyme Ero1p produces disulfide bonds for oxidative protein | + | The flavoenzyme Ero1p produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum. Disulfides generated de novo within Ero1p are transferred to protein disulfide isomerase and then to substrate proteins by dithiol-disulfide exchange reactions. Despite this key role of Ero1p, little is known about the mechanism by which this enzyme catalyzes thiol oxidation. Here, we present the X-ray crystallographic structure of Ero1p, which reveals the molecular details of the catalytic center, the role of a CXXCXXC motif, and the spatial relationship between functionally significant cysteines and the bound cofactor. Remarkably, the Ero1p active site closely resembles that of the versatile thiol oxidase module of Erv2p, a protein with no sequence homology to Ero1p. Furthermore, both Ero1p and Erv2p display essential dicysteine motifs on mobile polypeptide segments, suggesting that shuttling electrons to a rigid active site using a flexible strand is a fundamental feature of disulfide-generating flavoenzymes. |
==About this Structure== | ==About this Structure== | ||
| - | 1RQ1 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 CD, NEN and FAD as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1RQ1 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=CD:'>CD</scene>, <scene name='pdbligand=NEN:'>NEN</scene> and <scene name='pdbligand=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQ1 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Fass, D.]] | [[Category: Fass, D.]] | ||
[[Category: Gross, E.]] | [[Category: Gross, E.]] | ||
| - | [[Category: Kaiser, C | + | [[Category: Kaiser, C A.]] |
| - | [[Category: Kastner, D | + | [[Category: Kastner, D B.]] |
[[Category: CD]] | [[Category: CD]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: flavoenzyme]] | [[Category: flavoenzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:22 2008'' |
Revision as of 12:53, 21 February 2008
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Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell
Overview
The flavoenzyme Ero1p produces disulfide bonds for oxidative protein folding in the endoplasmic reticulum. Disulfides generated de novo within Ero1p are transferred to protein disulfide isomerase and then to substrate proteins by dithiol-disulfide exchange reactions. Despite this key role of Ero1p, little is known about the mechanism by which this enzyme catalyzes thiol oxidation. Here, we present the X-ray crystallographic structure of Ero1p, which reveals the molecular details of the catalytic center, the role of a CXXCXXC motif, and the spatial relationship between functionally significant cysteines and the bound cofactor. Remarkably, the Ero1p active site closely resembles that of the versatile thiol oxidase module of Erv2p, a protein with no sequence homology to Ero1p. Furthermore, both Ero1p and Erv2p display essential dicysteine motifs on mobile polypeptide segments, suggesting that shuttling electrons to a rigid active site using a flexible strand is a fundamental feature of disulfide-generating flavoenzymes.
About this Structure
1RQ1 is a Single protein structure of sequence from Saccharomyces cerevisiae with , and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of Ero1p, source of disulfide bonds for oxidative protein folding in the cell., Gross E, Kastner DB, Kaiser CA, Fass D, Cell. 2004 May 28;117(5):601-10. PMID:15163408
Page seeded by OCA on Thu Feb 21 14:53:22 2008
Categories: Saccharomyces cerevisiae | Single protein | Fass, D. | Gross, E. | Kaiser, C A. | Kastner, D B. | CD | FAD | NEN | Cxxcxxc | Disulfide bonds | Flavoenzyme
