|
|
| Line 1: |
Line 1: |
| | | | |
| | ==Solution structure of Cu(I) human Sco2== | | ==Solution structure of Cu(I) human Sco2== |
| - | <StructureSection load='2rli' size='340' side='right'caption='[[2rli]], [[NMR_Ensembles_of_Models | 31 NMR models]]' scene=''> | + | <StructureSection load='2rli' size='340' side='right'caption='[[2rli]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2rli]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2rli]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RLI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RLI FirstGlance]. <br> |
| - | </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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SCO2 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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'>[https://proteopedia.org/fgij/fg.htm?mol=2rli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rli OCA], [https://pdbe.org/2rli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rli RCSB], [https://www.ebi.ac.uk/pdbsum/2rli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rli 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=2rli FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rli OCA], [https://pdbe.org/2rli PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rli RCSB], [https://www.ebi.ac.uk/pdbsum/2rli PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rli ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[https://www.uniprot.org/uniprot/SCO2_HUMAN SCO2_HUMAN]] Defects in SCO2 are the cause of fatal infantile cardioencephalomyopathy with cytochrome c oxidase deficiency (FIC) [MIM:[https://omim.org/entry/604377 604377]]. This disease is characterized by hypertrophic cardiomyopathy, lactic acidosis, and gliosis. Heart and skeletal muscle show reductions in cytochrome c oxidase (COX) activity, whereas liver and fibroblasts show mild COX deficiencies.<ref>PMID:10545952</ref> <ref>PMID:10749987</ref> <ref>PMID:11673586</ref>
| + | [https://www.uniprot.org/uniprot/SCO2_HUMAN SCO2_HUMAN] Defects in SCO2 are the cause of fatal infantile cardioencephalomyopathy with cytochrome c oxidase deficiency (FIC) [MIM:[https://omim.org/entry/604377 604377]. This disease is characterized by hypertrophic cardiomyopathy, lactic acidosis, and gliosis. Heart and skeletal muscle show reductions in cytochrome c oxidase (COX) activity, whereas liver and fibroblasts show mild COX deficiencies.<ref>PMID:10545952</ref> <ref>PMID:10749987</ref> <ref>PMID:11673586</ref> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/SCO2_HUMAN SCO2_HUMAN]] Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2).
| + | [https://www.uniprot.org/uniprot/SCO2_HUMAN SCO2_HUMAN] Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
| Line 35: |
Line 35: |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Banci L]] |
| - | [[Category: Bertini, I]] | + | [[Category: Bertini I]] |
| - | [[Category: Ciofi-baffoni, S]] | + | [[Category: Ciofi-baffoni S]] |
| - | [[Category: Gerothanassis, I P]] | + | [[Category: Gerothanassis IP]] |
| - | [[Category: Leontari, I]] | + | [[Category: Leontari I]] |
| - | [[Category: Martinelli, M]] | + | [[Category: Martinelli M]] |
| - | [[Category: SPINE, Structural Proteomics in Europe]]
| + | [[Category: Wang S]] |
| - | [[Category: SPINE-2, Structural Proteomics in Europe 2]]
| + | |
| - | [[Category: Wang, S]] | + | |
| - | [[Category: Copper protein]]
| + | |
| - | [[Category: Metal transport]]
| + | |
| - | [[Category: Spine]]
| + | |
| - | [[Category: Spine-2]]
| + | |
| - | [[Category: Spine2-complex]]
| + | |
| - | [[Category: Structural genomic]]
| + | |
| - | [[Category: Structural proteomics in europe]]
| + | |
| - | [[Category: Structural proteomics in europe 2]]
| + | |
| - | [[Category: Thioredoxin fold]]
| + | |
| Structural highlights
Disease
SCO2_HUMAN Defects in SCO2 are the cause of fatal infantile cardioencephalomyopathy with cytochrome c oxidase deficiency (FIC) [MIM:604377. This disease is characterized by hypertrophic cardiomyopathy, lactic acidosis, and gliosis. Heart and skeletal muscle show reductions in cytochrome c oxidase (COX) activity, whereas liver and fibroblasts show mild COX deficiencies.[1] [2] [3]
Function
SCO2_HUMAN Acts as a copper chaperone, transporting copper to the Cu(A) site on the cytochrome c oxidase subunit II (COX2).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human Sco2 is a mitochondrial membrane-bound protein involved in copper supply for the assembly of cytochrome c oxidase in eukaryotes. Its precise action is not yet understood. We report here a structural and dynamic characterization by NMR of the apo and copper(I) forms of the soluble fragment. The structural and metal binding features of human Cu(I)Sco2 are similar to the more often studied Sco1 homolog, although the dynamic properties and the conformational disorder are quite different when the apo forms and the copper(I)-loaded forms of the two proteins are compared separately. Such differences are accounted for in terms of the different physicochemical properties in strategic protein locations. The misfunction of the known pathogenic mutations is discussed on the basis of the obtained structure.
A structural characterization of human SCO2.,Banci L, Bertini I, Ciofi-Baffoni S, Gerothanassis IP, Leontari I, Martinelli M, Wang S Structure. 2007 Sep;15(9):1132-40. PMID:17850752[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Papadopoulou LC, Sue CM, Davidson MM, Tanji K, Nishino I, Sadlock JE, Krishna S, Walker W, Selby J, Glerum DM, Coster RV, Lyon G, Scalais E, Lebel R, Kaplan P, Shanske S, De Vivo DC, Bonilla E, Hirano M, DiMauro S, Schon EA. Fatal infantile cardioencephalomyopathy with COX deficiency and mutations in SCO2, a COX assembly gene. Nat Genet. 1999 Nov;23(3):333-7. PMID:10545952 doi:10.1038/15513
- ↑ Jaksch M, Ogilvie I, Yao J, Kortenhaus G, Bresser HG, Gerbitz KD, Shoubridge EA. Mutations in SCO2 are associated with a distinct form of hypertrophic cardiomyopathy and cytochrome c oxidase deficiency. Hum Mol Genet. 2000 Mar 22;9(5):795-801. PMID:10749987
- ↑ Jaksch M, Horvath R, Horn N, Auer DP, Macmillan C, Peters J, Gerbitz KD, Kraegeloh-Mann I, Muntau A, Karcagi V, Kalmanchey R, Lochmuller H, Shoubridge EA, Freisinger P. Homozygosity (E140K) in SCO2 causes delayed infantile onset of cardiomyopathy and neuropathy. Neurology. 2001 Oct 23;57(8):1440-6. PMID:11673586
- ↑ Banci L, Bertini I, Ciofi-Baffoni S, Gerothanassis IP, Leontari I, Martinelli M, Wang S. A structural characterization of human SCO2. Structure. 2007 Sep;15(9):1132-40. PMID:17850752 doi:http://dx.doi.org/10.1016/j.str.2007.07.011
|
