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| | <StructureSection load='6n5u' size='340' side='right'caption='[[6n5u]], [[Resolution|resolution]] 2.66Å' scene=''> | | <StructureSection load='6n5u' size='340' side='right'caption='[[6n5u]], [[Resolution|resolution]] 2.66Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6n5u]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N5U OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6N5U FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6n5u]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6N5U OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6N5U FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</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]] 2.66Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HCC1, SCO1-1, At3g08950, T16O11.9 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CU1:COPPER+(I)+ION'>CU1</scene></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=6n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n5u OCA], [http://pdbe.org/6n5u PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6n5u RCSB], [http://www.ebi.ac.uk/pdbsum/6n5u PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6n5u 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=6n5u FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6n5u OCA], [https://pdbe.org/6n5u PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6n5u RCSB], [https://www.ebi.ac.uk/pdbsum/6n5u PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6n5u ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SCO11_ARATH SCO11_ARATH]] Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. Plays an essential role in embryo development.<ref>PMID:21041373</ref> <ref>PMID:21543521</ref> | + | [https://www.uniprot.org/uniprot/SCO11_ARATH SCO11_ARATH] Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. Plays an essential role in embryo development.<ref>PMID:21041373</ref> <ref>PMID:21543521</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Alzari, P M]] | + | [[Category: Alzari PM]] |
| - | [[Category: Giannini, E]] | + | [[Category: Giannini E]] |
| - | [[Category: Lisa, M N]] | + | [[Category: Lisa MN]] |
| - | [[Category: Llases, M E]] | + | [[Category: Llases ME]] |
| - | [[Category: Vila, A J]] | + | [[Category: Vila AJ]] |
| - | [[Category: Hcc1]]
| + | |
| - | [[Category: Metal binding protein]]
| + | |
| - | [[Category: Metal ion]]
| + | |
| - | [[Category: Metallochaperone]]
| + | |
| - | [[Category: Reduced form]]
| + | |
| - | [[Category: Thioredoxin fold]]
| + | |
| Structural highlights
Function
SCO11_ARATH Thought to play a role in cellular copper homeostasis, mitochondrial redox signaling or insertion of copper into the active site of COX. Plays an essential role in embryo development.[1] [2]
Publication Abstract from PubMed
The assembly of the CuA site in Cytochrome c Oxidase (COX) is a critical step for aerobic respiration in COX-dependent organisms. Several gene products have been associated with the assembly of this copper site, the most conserved of them belonging to the Sco family of proteins, which have been shown to perform different roles in different organisms. Plants express two orthologs of Sco proteins: Hcc1 and Hcc2. Hcc1 is known to be essential for plant development and for COX maturation, but its precise function has not been addressed until now. Here, we report the biochemical, structural and functional characterization of Arabidopsis thaliana Hcc1 protein (here renamed Sco1). We solved the crystal structure of the Cu(+1) -bound soluble domain of this protein, revealing a tri coordinated environment involving a CxxxCxn H motif. We show that AtSco1 is able to work as a copper metallochaperone, inserting two Cu(+1) ions into the CuA site in a model of CoxII. We also show that AtSco1 does not act as a thiol-disulfide oxido-reductase. Overall, this information sheds new light on the biochemistry of Sco proteins, highlighting the diversity of functions among them despite their high structural similarities. DATABASE: PDB entry 6N5U (Crystal structure of Arabidopsis thaliana ScoI with copper bound).
Arabidopsis thaliana Hcc1 is a Sco-like metallochaperone for CuA assembly in Cytochrome c Oxidase.,Llases ME, Lisa MN, Morgada MN, Giannini E, Alzari PM, Vila AJ FEBS J. 2019 Jul 26. doi: 10.1111/febs.15016. PMID:31348612[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Steinebrunner I, Landschreiber M, Krause-Buchholz U, Teichmann J, Rodel G. HCC1, the Arabidopsis homologue of the yeast mitochondrial copper chaperone SCO1, is essential for embryonic development. J Exp Bot. 2011 Jan;62(1):319-30. doi: 10.1093/jxb/erq269. Epub 2010 Nov 1. PMID:21041373 doi:http://dx.doi.org/10.1093/jxb/erq269
- ↑ Attallah CV, Welchen E, Martin AP, Spinelli SV, Bonnard G, Palatnik JF, Gonzalez DH. Plants contain two SCO proteins that are differentially involved in cytochrome c oxidase function and copper and redox homeostasis. J Exp Bot. 2011 Aug;62(12):4281-94. doi: 10.1093/jxb/err138. Epub 2011 May 4. PMID:21543521 doi:http://dx.doi.org/10.1093/jxb/err138
- ↑ Llases ME, Lisa MN, Morgada MN, Giannini E, Alzari PM, Vila AJ. Arabidopsis thaliana Hcc1 is a Sco-like metallochaperone for CuA assembly in Cytochrome c Oxidase. FEBS J. 2019 Jul 26. doi: 10.1111/febs.15016. PMID:31348612 doi:http://dx.doi.org/10.1111/febs.15016
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