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[[Image:1jra.jpg|left|200px]]
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{{STRUCTURE_1jra|  PDB=1jra  |  SCENE=  }}
'''Crystal Structure of Erv2p'''


==Crystal Structure of Erv2p==
<StructureSection load='1jra' size='340' side='right'caption='[[1jra]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1jra]] is a 4 chain structure with sequence from [https://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]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JRA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jra FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jra OCA], [https://pdbe.org/1jra PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jra RCSB], [https://www.ebi.ac.uk/pdbsum/1jra PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jra ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ERV2_YEAST ERV2_YEAST] FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1.<ref>PMID:11313344</ref> <ref>PMID:11584268</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jr/1jra_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1jra ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:11740506</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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].
</div>
<div class="pdbe-citations 1jra" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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]
*[[Sulfhydryl oxidase 3D structures|Sulfhydryl oxidase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Fass D]]
[[Category: Fass, D.]]
[[Category: Gross E]]
[[Category: Gross, E.]]
[[Category: Kaiser CA]]
[[Category: Kaiser, C A.]]
[[Category: Sevier CS]]
[[Category: Sevier, C S.]]
[[Category: Vala A]]
[[Category: Vala, A.]]
[[Category: Cxxc]]
[[Category: Fad]]
[[Category: Helical bundle]]
[[Category: Sulfhydryl oxidase]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 21:44:28 2008''
Retrieved from "https://proteopedia.org/1jra"