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| - | {{STRUCTURE_3uo3| PDB=3uo3 | SCENE= }} | |
| - | ===Jac1 co-chaperone from Saccharomyces cerevisiae, 5-182 clone=== | |
| - | {{ABSTRACT_PUBMED_22306468}} | |
| | | | |
| - | ==Function== | + | ==Jac1 co-chaperone from Saccharomyces cerevisiae, 5-182 clone== |
| - | [[http://www.uniprot.org/uniprot/JAC1_YEAST JAC1_YEAST]] Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of its specialized Hsp70 chaperone partner SSQ1. Binds to the substrate protein ISU1 and targets it to SSQ1. May function together with SSQ1 in the dislocation of the Fe/S cluster from ISU1 and its insertion into apoproteins.<ref>PMID:11171977</ref> <ref>PMID:9813017</ref> <ref>PMID:11278728</ref> <ref>PMID:11273703</ref> <ref>PMID:12970193</ref> <ref>PMID:12756240</ref> <ref>PMID:15123690</ref> <ref>PMID:16431909</ref> <ref>PMID:16551614</ref> | + | <StructureSection load='3uo3' size='340' side='right'caption='[[3uo3]], [[Resolution|resolution]] 1.85Å' scene=''> |
| - | | + | == Structural highlights == |
| - | ==About this Structure== | + | <table><tr><td colspan='2'>[[3uo3]] is a 2 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=3UO3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3UO3 FirstGlance]. <br> |
| - | [[3uo3]] is a 2 chain structure with sequence from [http://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=3UO3 OCA].
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85Å</td></tr> |
| - | | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene></td></tr> |
| - | ==Reference==
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3uo3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3uo3 OCA], [https://pdbe.org/3uo3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3uo3 RCSB], [https://www.ebi.ac.uk/pdbsum/3uo3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3uo3 ProSAT]</span></td></tr> |
| - | <ref group="xtra">PMID:022306468</ref><references group="xtra"/><references/>
| + | </table> |
| - | [[Category: Saccharomyces cerevisiae s288c]] | + | == Function == |
| - | [[Category: Babnigg, G.]] | + | [https://www.uniprot.org/uniprot/JAC1_YEAST JAC1_YEAST] Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of its specialized Hsp70 chaperone partner SSQ1. Binds to the substrate protein ISU1 and targets it to SSQ1. May function together with SSQ1 in the dislocation of the Fe/S cluster from ISU1 and its insertion into apoproteins.<ref>PMID:11171977</ref> <ref>PMID:9813017</ref> <ref>PMID:11278728</ref> <ref>PMID:11273703</ref> <ref>PMID:12970193</ref> <ref>PMID:12756240</ref> <ref>PMID:15123690</ref> <ref>PMID:16431909</ref> <ref>PMID:16551614</ref> |
| - | [[Category: Bigelow, L.]] | + | == References == |
| - | [[Category: Craig, E A.]] | + | <references/> |
| - | [[Category: Dutkiewicz, R.]] | + | __TOC__ |
| - | [[Category: Feldmann, B.]] | + | </StructureSection> |
| - | [[Category: Joachimiak, A.]] | + | [[Category: Large Structures]] |
| - | [[Category: MCSG, Midwest Center for Structural Genomics.]]
| + | [[Category: Saccharomyces cerevisiae S288C]] |
| - | [[Category: Marszalek, J.]] | + | [[Category: Babnigg G]] |
| - | [[Category: Mulligan, R.]] | + | [[Category: Bigelow L]] |
| - | [[Category: Osipiuk, J.]] | + | [[Category: Craig EA]] |
| - | [[Category: Chaperone]]
| + | [[Category: Dutkiewicz R]] |
| - | [[Category: Co-chaperone]]
| + | [[Category: Feldmann B]] |
| - | [[Category: Iron sulfur cluster biogenesis]]
| + | [[Category: Joachimiak A]] |
| - | [[Category: Isu protein]]
| + | [[Category: Marszalek J]] |
| - | [[Category: J-protein]]
| + | [[Category: Mulligan R]] |
| - | [[Category: Mcsg]]
| + | [[Category: Osipiuk J]] |
| - | [[Category: Midwest center for structural genomic]]
| + | |
| - | [[Category: Psi-biology]]
| + | |
| - | [[Category: Ssq1 hsp70 chaperone]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| Structural highlights
Function
JAC1_YEAST Co-chaperone required for the assembly of iron-sulfur (Fe/S) clusters in mitochondria. Stimulates the ATPase activity of its specialized Hsp70 chaperone partner SSQ1. Binds to the substrate protein ISU1 and targets it to SSQ1. May function together with SSQ1 in the dislocation of the Fe/S cluster from ISU1 and its insertion into apoproteins.[1] [2] [3] [4] [5] [6] [7] [8] [9]
References
- ↑ Voisine C, Cheng YC, Ohlson M, Schilke B, Hoff K, Beinert H, Marszalek J, Craig EA. Jac1, a mitochondrial J-type chaperone, is involved in the biogenesis of Fe/S clusters in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A. 2001 Feb 13;98(4):1483-8. PMID:11171977 doi:10.1073/pnas.98.4.1483
- ↑ Strain J, Lorenz CR, Bode J, Garland S, Smolen GA, Ta DT, Vickery LE, Culotta VC. Suppressors of superoxide dismutase (SOD1) deficiency in Saccharomyces cerevisiae. Identification of proteins predicted to mediate iron-sulfur cluster assembly. J Biol Chem. 1998 Nov 20;273(47):31138-44. PMID:9813017
- ↑ Kim R, Saxena S, Gordon DM, Pain D, Dancis A. J-domain protein, Jac1p, of yeast mitochondria required for iron homeostasis and activity of Fe-S cluster proteins. J Biol Chem. 2001 May 18;276(20):17524-32. Epub 2001 Feb 27. PMID:11278728 doi:10.1074/jbc.M010695200
- ↑ Lutz T, Westermann B, Neupert W, Herrmann JM. The mitochondrial proteins Ssq1 and Jac1 are required for the assembly of iron sulfur clusters in mitochondria. J Mol Biol. 2001 Mar 30;307(3):815-25. PMID:11273703 doi:10.1006/jmbi.2001.4527
- ↑ Muhlenhoff U, Gerber J, Richhardt N, Lill R. Components involved in assembly and dislocation of iron-sulfur clusters on the scaffold protein Isu1p. EMBO J. 2003 Sep 15;22(18):4815-25. PMID:12970193 doi:http://dx.doi.org/10.1093/emboj/cdg446
- ↑ Dutkiewicz R, Schilke B, Knieszner H, Walter W, Craig EA, Marszalek J. Ssq1, a mitochondrial Hsp70 involved in iron-sulfur (Fe/S) center biogenesis. Similarities to and differences from its bacterial counterpart. J Biol Chem. 2003 Aug 8;278(32):29719-27. Epub 2003 May 19. PMID:12756240 doi:10.1074/jbc.M303527200
- ↑ Dutkiewicz R, Schilke B, Cheng S, Knieszner H, Craig EA, Marszalek J. Sequence-specific interaction between mitochondrial Fe-S scaffold protein Isu and Hsp70 Ssq1 is essential for their in vivo function. J Biol Chem. 2004 Jul 9;279(28):29167-74. Epub 2004 Apr 30. PMID:15123690 doi:10.1074/jbc.M402947200
- ↑ Dutkiewicz R, Marszalek J, Schilke B, Craig EA, Lill R, Muhlenhoff U. The Hsp70 chaperone Ssq1p is dispensable for iron-sulfur cluster formation on the scaffold protein Isu1p. J Biol Chem. 2006 Mar 24;281(12):7801-8. Epub 2006 Jan 23. PMID:16431909 doi:M513301200
- ↑ Andrew AJ, Dutkiewicz R, Knieszner H, Craig EA, Marszalek J. Characterization of the interaction between the J-protein Jac1p and the scaffold for Fe-S cluster biogenesis, Isu1p. J Biol Chem. 2006 May 26;281(21):14580-7. Epub 2006 Mar 21. PMID:16551614 doi:10.1074/jbc.M600842200
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