1rq1

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[[Image:1rq1.jpg|left|200px]]<br /><applet load="1rq1" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1rq1.jpg|left|200px]]
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caption="1rq1, resolution 2.8&Aring;" />
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'''Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell'''<br />
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{{Structure
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|PDB= 1rq1 |SIZE=350|CAPTION= <scene name='initialview01'>1rq1</scene>, resolution 2.8&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene>, <scene name='pdbligand=NEN:1-ETHYL-PYRROLIDINE-2,5-DIONE'>NEN</scene> and <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene>
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|ACTIVITY=
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|GENE= YML130C, YM4987.05C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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1RQ1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RQ1 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15163408 15163408]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/15163408 15163408]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: NEN]]
[[Category: NEN]]
[[Category: cxxcxxc]]
[[Category: cxxcxxc]]
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[[Category: disulfide bonds]]
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[[Category: disulfide bond]]
[[Category: flavoenzyme]]
[[Category: flavoenzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:54:47 2008''

Revision as of 11:54, 20 March 2008


PDB ID 1rq1

Drag the structure with the mouse to rotate
, resolution 2.8Å
Ligands: , and
Gene: YML130C, YM4987.05C (Saccharomyces cerevisiae)
Coordinates: save as pdb, mmCIF, xml



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. 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

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