1jra: Difference between revisions
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[[Image:1jra.jpg|left|200px]] | [[Image:1jra.jpg|left|200px]] | ||
'''Crystal Structure of Erv2p''' | {{Structure | ||
|PDB= 1jra |SIZE=350|CAPTION= <scene name='initialview01'>1jra</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | |||
|ACTIVITY= | |||
|GENE= ERV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |||
}} | |||
'''Crystal Structure of Erv2p''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1JRA is a [ | 1JRA 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=1JRA OCA]. | ||
==Reference== | ==Reference== | ||
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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11740506 11740506] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: sulfhydryl oxidase]] | [[Category: sulfhydryl oxidase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:07:22 2008'' |
Revision as of 13:07, 20 March 2008
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, resolution 2.0Å | |||||||
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Ligands: | |||||||
Gene: | ERV2 (Saccharomyces cerevisiae) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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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