1jra: Difference between revisions

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[[Image:1jra.jpg|left|200px]]
[[Image:1jra.jpg|left|200px]]


{{Structure
<!--
|PDB= 1jra |SIZE=350|CAPTION= <scene name='initialview01'>1jra</scene>, resolution 2.0&Aring;
The line below this paragraph, containing "STRUCTURE_1jra", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=  
or leave the SCENE parameter empty for the default display.
|GENE= ERV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
-->
|DOMAIN=
{{STRUCTURE_1jra| PDB=1jra  | SCENE= }}  
|RELATEDENTRY=[[1jr8|1JR8]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jra OCA], [http://www.ebi.ac.uk/pdbsum/1jra PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jra RCSB]</span>
}}


'''Crystal Structure of Erv2p'''
'''Crystal Structure of Erv2p'''
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[[Category: Sevier, C S.]]
[[Category: Sevier, C S.]]
[[Category: Vala, A.]]
[[Category: Vala, A.]]
[[Category: cxxc]]
[[Category: Cxxc]]
[[Category: fad]]
[[Category: Fad]]
[[Category: helical bundle]]
[[Category: Helical bundle]]
[[Category: sulfhydryl oxidase]]
[[Category: Sulfhydryl oxidase]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:44:28 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:37:51 2008''

Revision as of 21:44, 2 May 2008

File:1jra.jpg

Template:STRUCTURE 1jra

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 Page seeded by OCA on Fri May 2 21:44:28 2008

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