1jra: Difference between revisions

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[[Image:1jra.jpg|left|200px]]
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{{STRUCTURE_1jra|  PDB=1jra  |  SCENE=  }}  
{{STRUCTURE_1jra|  PDB=1jra  |  SCENE=  }}  


'''Crystal Structure of Erv2p'''
===Crystal Structure of Erv2p===




==Overview==
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Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide bond formation during protein biosynthesis in the yeast endoplasmic reticulum. The structure of Erv2p, determined by X-ray crystallography to 1.5 A resolution, reveals a helix-rich dimer with no global resemblance to other known FAD-binding proteins or thiol oxidoreductases. Two pairs of cysteine residues are required for Erv2p activity. The first (Cys-Gly-Glu-Cys) is adjacent to the isoalloxazine ring of the FAD. The second (Cys-Gly-Cys) is part of a flexible C-terminal segment that can swing into the vicinity of the first cysteine pair in the opposite subunit of the dimer and may shuttle electrons between substrate protein dithiols and the FAD-proximal disulfide.
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{{ABSTRACT_PUBMED_11740506}}


==About this Structure==
==About this Structure==
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[[Category: Helical bundle]]
[[Category: Helical bundle]]
[[Category: Sulfhydryl oxidase]]
[[Category: Sulfhydryl oxidase]]
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Revision as of 20:41, 1 July 2008

File:1jra.png

Template:STRUCTURE 1jra

Crystal Structure of Erv2pCrystal Structure of Erv2p

Template:ABSTRACT PUBMED 11740506

About this StructureAbout this Structure

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

ReferenceReference

A new FAD-binding fold and intersubunit disulfide shuttle in the thiol oxidase Erv2p., Gross E, Sevier CS, Vala A, Kaiser CA, Fass D, Nat Struct Biol. 2002 Jan;9(1):61-7. PMID:11740506

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