1jra: Difference between revisions
New page: left|200px<br /><applet load="1jra" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jra, resolution 2.0Å" /> '''Crystal Structure of ... |
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[[Image:1jra.jpg|left|200px]]<br /><applet load="1jra" size=" | [[Image:1jra.jpg|left|200px]]<br /><applet load="1jra" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1jra, resolution 2.0Å" /> | caption="1jra, resolution 2.0Å" /> | ||
'''Crystal Structure of Erv2p'''<br /> | '''Crystal Structure of Erv2p'''<br /> | ||
==Overview== | ==Overview== | ||
Erv2p is an FAD-dependent sulfhydryl oxidase that can promote disulfide | 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. | ||
==About this Structure== | ==About this Structure== | ||
1JRA 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 FAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1JRA 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=FAD:'>FAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRA 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: Sevier, C | [[Category: Sevier, C S.]] | ||
[[Category: Vala, A.]] | [[Category: Vala, A.]] | ||
[[Category: FAD]] | [[Category: FAD]] | ||
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[[Category: sulfhydryl oxidase]] | [[Category: sulfhydryl oxidase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:50 2008'' | ||
Revision as of 14:25, 21 February 2008
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Crystal Structure of Erv2p
OverviewOverview
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.
About this StructureAbout this Structure
1JRA is a Single protein structure of sequence from Saccharomyces cerevisiae with as ligand. 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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