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| <StructureSection load='3w4y' size='340' side='right'caption='[[3w4y]], [[Resolution|resolution]] 2.00Å' scene=''> | | <StructureSection load='3w4y' size='340' side='right'caption='[[3w4y]], [[Resolution|resolution]] 2.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[3w4y]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Baker's_yeast Baker's yeast]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W4Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3w4y]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3W4Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3W4Y FirstGlance]. <br> |
- | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
- | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[4eoh|4eoh]], [[4eoi|4eoi]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERV1, ERV1/YGR029W, YGR029W ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr> | + | |
- | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.3.2 1.8.3.2] </span></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=3w4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w4y OCA], [https://pdbe.org/3w4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w4y RCSB], [https://www.ebi.ac.uk/pdbsum/3w4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w4y ProSAT]</span></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=3w4y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3w4y OCA], [https://pdbe.org/3w4y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3w4y RCSB], [https://www.ebi.ac.uk/pdbsum/3w4y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3w4y ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[https://www.uniprot.org/uniprot/ERV1_YEAST ERV1_YEAST]] FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.[PROSITE-ProRule:PRU00654]<ref>PMID:10899311</ref> <ref>PMID:11493598</ref> <ref>PMID:12654008</ref> <ref>PMID:15989955</ref> <ref>PMID:16181637</ref> <ref>PMID:16185707</ref>
| + | [https://www.uniprot.org/uniprot/ERV1_YEAST ERV1_YEAST] FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.[PROSITE-ProRule:PRU00654]<ref>PMID:10899311</ref> <ref>PMID:11493598</ref> <ref>PMID:12654008</ref> <ref>PMID:15989955</ref> <ref>PMID:16181637</ref> <ref>PMID:16185707</ref> |
| | | |
| ==See Also== | | ==See Also== |
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| __TOC__ | | __TOC__ |
| </StructureSection> | | </StructureSection> |
- | [[Category: Baker's yeast]] | |
| [[Category: Large Structures]] | | [[Category: Large Structures]] |
- | [[Category: Thiol oxidase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
- | [[Category: Endo, T]] | + | [[Category: Endo T]] |
- | [[Category: Kawano, S]] | + | [[Category: Kawano S]] |
- | [[Category: Terao, K]] | + | [[Category: Terao K]] |
- | [[Category: Watanabe, N]] | + | [[Category: Watanabe N]] |
- | [[Category: Alpha helix]]
| + | |
- | [[Category: Disulfide bond]]
| + | |
- | [[Category: Mitochondria]]
| + | |
- | [[Category: Oxidoreductase]]
| + | |
- | [[Category: Redox]]
| + | |
- | [[Category: Tim40/mia40]]
| + | |
| Structural highlights
Function
ERV1_YEAST FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation. Required for the import and folding of small cysteine-containing proteins in the mitochondrial intermembrane space (IMS). Forms a redox cycle with MIA40 that involves a disulfide relay system. Important for maintaining the cysteine residues in MIA40 in an oxidized state. Reduced ERV1 is reoxidized by cytochrome c. Required for the maturation of cytoplasmic, but not of mitochondrial Fe/S proteins.[PROSITE-ProRule:PRU00654][1] [2] [3] [4] [5] [6]
See Also
References
- ↑ Lee J, Hofhaus G, Lisowsky T. Erv1p from Saccharomyces cerevisiae is a FAD-linked sulfhydryl oxidase. FEBS Lett. 2000 Jul 14;477(1-2):62-6. PMID:10899311
- ↑ Lange H, Lisowsky T, Gerber J, Muhlenhoff U, Kispal G, Lill R. An essential function of the mitochondrial sulfhydryl oxidase Erv1p/ALR in the maturation of cytosolic Fe/S proteins. EMBO Rep. 2001 Aug;2(8):715-20. PMID:11493598 doi:http://dx.doi.org/10.1093/embo-reports/kve161
- ↑ Hofhaus G, Lee JE, Tews I, Rosenberg B, Lisowsky T. The N-terminal cysteine pair of yeast sulfhydryl oxidase Erv1p is essential for in vivo activity and interacts with the primary redox centre. Eur J Biochem. 2003 Apr;270(7):1528-35. PMID:12654008
- ↑ Mesecke N, Terziyska N, Kozany C, Baumann F, Neupert W, Hell K, Herrmann JM. A disulfide relay system in the intermembrane space of mitochondria that mediates protein import. Cell. 2005 Jul 1;121(7):1059-69. PMID:15989955 doi:http://dx.doi.org/S0092-8674(05)00357-0
- ↑ Rissler M, Wiedemann N, Pfannschmidt S, Gabriel K, Guiard B, Pfanner N, Chacinska A. The essential mitochondrial protein Erv1 cooperates with Mia40 in biogenesis of intermembrane space proteins. J Mol Biol. 2005 Oct 28;353(3):485-92. Epub 2005 Sep 8. PMID:16181637 doi:http://dx.doi.org/10.1016/j.jmb.2005.08.051
- ↑ Allen S, Balabanidou V, Sideris DP, Lisowsky T, Tokatlidis K. Erv1 mediates the Mia40-dependent protein import pathway and provides a functional link to the respiratory chain by shuttling electrons to cytochrome c. J Mol Biol. 2005 Nov 11;353(5):937-44. Epub 2005 Sep 15. PMID:16185707 doi:http://dx.doi.org/S0022-2836(05)01003-X
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