3m31

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{{STRUCTURE_3m31| PDB=3m31 | SCENE= }}
{{STRUCTURE_3m31| PDB=3m31 | SCENE= }}
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===Structure of the C150A/C295A mutant of S. cerevisiae Ero1p===
===Structure of the C150A/C295A mutant of S. cerevisiae Ero1p===
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{{ABSTRACT_PUBMED_20669236}}
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==Function==
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[[http://www.uniprot.org/uniprot/ERO1_YEAST ERO1_YEAST]] Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.<ref>PMID:9659913</ref> <ref>PMID:9659914</ref> <ref>PMID:10549279</ref> <ref>PMID:11090354</ref> <ref>PMID:12453408</ref>
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{{ABSTRACT_PUBMED_20669236}}
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==About this Structure==
==About this Structure==
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3M31 is a 1 chain structure with 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=3M31 OCA].
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[[3m31]] is a 1 chain structure with 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=3M31 OCA].
==Reference==
==Reference==
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<ref group="xtra">PMID:20669236</ref><references group="xtra"/>
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<ref group="xtra">PMID:020669236</ref><references group="xtra"/><references/>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Fass, D.]]
[[Category: Fass, D.]]
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[[Category: Redox-active center]]
[[Category: Redox-active center]]
[[Category: Transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Nov 3 11:09:54 2010''
 

Revision as of 23:22, 10 April 2013

Template:STRUCTURE 3m31

Contents

Structure of the C150A/C295A mutant of S. cerevisiae Ero1p

Template:ABSTRACT PUBMED 20669236

Function

[ERO1_YEAST] Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress.[1] [2] [3] [4] [5]

About this Structure

3m31 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

  • Heldman N, Vonshak O, Sevier CS, Vitu E, Mehlman T, Fass D. Steps in reductive activation of the disulfide-generating enzyme Ero1p. Protein Sci. 2010 Oct;19(10):1863-76. PMID:20669236 doi:10.1002/pro.473
  1. ↑ Frand AR, Kaiser CA. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol Cell. 1998 Jan;1(2):161-70. PMID:9659913
  2. ↑ Pollard MG, Travers KJ, Weissman JS. Ero1p: a novel and ubiquitous protein with an essential role in oxidative protein folding in the endoplasmic reticulum. Mol Cell. 1998 Jan;1(2):171-82. PMID:9659914
  3. ↑ Frand AR, Kaiser CA. Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell. 1999 Oct;4(4):469-77. PMID:10549279
  4. ↑ Tu BP, Ho-Schleyer SC, Travers KJ, Weissman JS. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science. 2000 Nov 24;290(5496):1571-4. PMID:11090354
  5. ↑ Tu BP, Weissman JS. The FAD- and O(2)-dependent reaction cycle of Ero1-mediated oxidative protein folding in the endoplasmic reticulum. Mol Cell. 2002 Nov;10(5):983-94. PMID:12453408

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