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| | ==Crystal structure of FAD binding domain of Erv1 from Saccharomyces cerevisiae== | | ==Crystal structure of FAD binding domain of Erv1 from Saccharomyces cerevisiae== |
| - | <StructureSection load='4e0h' size='340' side='right' caption='[[4e0h]], [[Resolution|resolution]] 2.00Å' scene=''> | + | <StructureSection load='4e0h' size='340' side='right'caption='[[4e0h]], [[Resolution|resolution]] 2.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4e0h]] is a 1 chain structure with sequence from [http://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=4E0H OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E0H FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4e0h]] is a 1 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=4E0H OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E0H FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FAD:FLAVIN-ADENINE+DINUCLEOTIDE'>FAD</scene></td></tr> | + | </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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1oqc|1oqc]], [[4e0i|4e0i]]</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=4e0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0h OCA], [https://pdbe.org/4e0h PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e0h RCSB], [https://www.ebi.ac.uk/pdbsum/4e0h PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e0h ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ERV1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=559292 Baker's yeast])</td></tr>
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| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Thiol_oxidase Thiol oxidase], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e0h FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e0h OCA], [http://pdbe.org/4e0h PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e0h RCSB], [http://www.ebi.ac.uk/pdbsum/4e0h PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4e0h ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Sulfhydryl oxidase|Sulfhydryl oxidase]] | + | *[[Sulfhydryl oxidase 3D structures|Sulfhydryl oxidase 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Baker's yeast]] | + | [[Category: Large Structures]] |
| - | [[Category: Thiol oxidase]] | + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Chen, Y X]] | + | [[Category: Chen YX]] |
| - | [[Category: Guo, P C]] | + | [[Category: Guo PC]] |
| - | [[Category: Hu, T T]] | + | [[Category: Hu TT]] |
| - | [[Category: Jiang, Y L]] | + | [[Category: Jiang YL]] |
| - | [[Category: Ma, J D]] | + | [[Category: Ma JD]] |
| - | [[Category: Wang, S J]] | + | [[Category: Wang SJ]] |
| - | [[Category: Zhou, C Z]] | + | [[Category: Zhou CZ]] |
| - | [[Category: Fad binding]]
| + | |
| - | [[Category: Flavin-linked sulfhydryl oxidase]]
| + | |
| - | [[Category: Four-helix bundle]]
| + | |
| - | [[Category: Mitochondrial intermembrane space]]
| + | |
| - | [[Category: Oxidation]]
| + | |
| - | [[Category: Oxidoreductase]]
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| 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]
Publication Abstract from PubMed
The disulfide relay system in the mitochondrial intermembrane space drives the import of proteins with twin CX(9)C or twin CX(3)C motifs by an oxidative folding mechanism. This process requires disulfide bond transfer from oxidized Mia40 to a substrate protein. Reduced Mia40 is reoxidized/regenerated by the FAD-linked sulfhydryl oxidase Erv1 (EC 1.8.3.2). Full-length Erv1 consists of a flexible N-terminal shuttle domain (NTD) and a conserved C-terminal core domain (CTD). Here, we present crystal structures at 2.0 A resolution of the CTD and at 3.0 A resolution of a C30S/C133S double mutant of full-length Erv1 (Erv1FL). Similar to previous homologous structures, the CTD exists as a homodimer, with each subunit consisting of a conserved four-helix bundle that accommodates the isoalloxazine ring of FAD and an additional single-turn helix. The structure of Erv1FL enabled us to identify, for the first time, the three-dimensional structure of the Erv1NTD, which is an amphipathic helix flanked by two flexible loops. This structure also represents an intermediate state of electron transfer from the NTD to the CTD of another subunit. Comparative structural analysis revealed that the four-helix bundle of the CTD forms a wide platform for the electron donor NTD. Moreover, computational simulation combined with multiple-sequence alignment suggested that the amphipathic helix close to the shuttle redox enter is critical for the recognition of Mia40, the upstream electron donor. These findings provide structural insights into electron transfer from Mia40 via the shuttle domain of one subunit of Erv1 to the CTD of another Erv1 subunit.
Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space.,Guo PC, Ma JD, Jiang YL, Wang SJ, Bao ZZ, Yu XJ, Chen Y, Zhou CZ J Biol Chem. 2012 Oct 12;287(42):34961-9. doi: 10.1074/jbc.M112.394759. Epub 2012, Aug 21. PMID:22910915[7]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
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
- ↑ Guo PC, Ma JD, Jiang YL, Wang SJ, Bao ZZ, Yu XJ, Chen Y, Zhou CZ. Structure of yeast sulfhydryl oxidase erv1 reveals electron transfer of the disulfide relay system in the mitochondrial intermembrane space. J Biol Chem. 2012 Oct 12;287(42):34961-9. doi: 10.1074/jbc.M112.394759. Epub 2012, Aug 21. PMID:22910915 doi:http://dx.doi.org/10.1074/jbc.M112.394759
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