1jr8

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<StructureSection load='1jr8' size='340' side='right'caption='[[1jr8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
<StructureSection load='1jr8' size='340' side='right'caption='[[1jr8]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1jr8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JR8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1JR8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1jr8]] is a 2 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=1JR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JR8 FirstGlance]. <br>
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</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>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.5&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERV2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1jr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr8 OCA], [http://pdbe.org/1jr8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jr8 RCSB], [http://www.ebi.ac.uk/pdbsum/1jr8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr8 ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jr8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr8 OCA], [https://pdbe.org/1jr8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jr8 RCSB], [https://www.ebi.ac.uk/pdbsum/1jr8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr8 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://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>
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[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</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=1jr8 ConSurf].
</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=1jr8 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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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.
 
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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>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1jr8" style="background-color:#fffaf0;"></div>
 
==See Also==
==See Also==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Atcc 18824]]
 
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Fass, D]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Gross, E]]
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[[Category: Fass D]]
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[[Category: Kaiser, C A]]
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[[Category: Gross E]]
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[[Category: Sevier, C S]]
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[[Category: Kaiser CA]]
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[[Category: Vala, A]]
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[[Category: Sevier CS]]
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[[Category: Cxxc]]
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[[Category: Vala A]]
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[[Category: Fad]]
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[[Category: Helical bundle]]
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[[Category: Oxidoreductase]]
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[[Category: Sulfhydryl oxidase]]
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Revision as of 07:54, 3 April 2024

Crystal Structure of Erv2p

PDB ID 1jr8

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