1jr8
From Proteopedia
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|PDB= 1jr8 |SIZE=350|CAPTION= <scene name='initialview01'>1jr8</scene>, resolution 1.5Å | |PDB= 1jr8 |SIZE=350|CAPTION= <scene name='initialview01'>1jr8</scene>, resolution 1.5Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE DINUCLEOTIDE'>FAD</scene> | + | |LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= ERV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= ERV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr8 OCA], [http://www.ebi.ac.uk/pdbsum/1jr8 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jr8 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sevier, C S.]] | [[Category: Sevier, C S.]] | ||
[[Category: Vala, A.]] | [[Category: Vala, A.]] | ||
| - | [[Category: FAD]] | ||
[[Category: cxxc]] | [[Category: cxxc]] | ||
[[Category: fad]] | [[Category: fad]] | ||
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[[Category: sulfhydryl oxidase]] | [[Category: sulfhydryl oxidase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:37:51 2008'' |
Revision as of 18:37, 30 March 2008
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| , resolution 1.5Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | ERV2 (Saccharomyces cerevisiae) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure of Erv2p
Overview
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
1JR8 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
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:11740506
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