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| | <StructureSection load='6qe3' size='340' side='right'caption='[[6qe3]], [[Resolution|resolution]] 1.75Å' scene=''> | | <StructureSection load='6qe3' size='340' side='right'caption='[[6qe3]], [[Resolution|resolution]] 1.75Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qe3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6esr 6esr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QE3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6QE3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6qe3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=6esr 6esr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QE3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QE3 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5oli|5oli]]</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]] 1.75Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">IBA57, C1orf69 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=6qe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qe3 OCA], [https://pdbe.org/6qe3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qe3 RCSB], [https://www.ebi.ac.uk/pdbsum/6qe3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qe3 ProSAT]</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=6qe3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qe3 OCA], [http://pdbe.org/6qe3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qe3 RCSB], [http://www.ebi.ac.uk/pdbsum/6qe3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qe3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/CAF17_HUMAN CAF17_HUMAN]] Hypotonia-cerebral atrophy-hyperglycinemia syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/CAF17_HUMAN CAF17_HUMAN] Hypotonia-cerebral atrophy-hyperglycinemia syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CAF17_HUMAN CAF17_HUMAN]] Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway.<ref>PMID:23462291</ref> | + | [https://www.uniprot.org/uniprot/CAF17_HUMAN CAF17_HUMAN] Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway.<ref>PMID:23462291</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6qe3" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6qe3" style="background-color:#fffaf0;"></div> |
| - | | |
| - | ==See Also== | |
| - | *[[Journal:Acta Cryst D:S2059798319000214|Journal:Acta Cryst D:S2059798319000214]] | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Banci, L]] | + | [[Category: Banci L]] |
| - | [[Category: Calderone, V]] | + | [[Category: Calderone V]] |
| - | [[Category: Ciofi-Baffoni, S]] | + | [[Category: Ciofi-Baffoni S]] |
| - | [[Category: Gourdoupis, S]] | + | [[Category: Gourdoupis S]] |
| - | [[Category: Fe-s protein biogenesis]]
| + | |
| - | [[Category: Infantile leukodystrophy]]
| + | |
| - | [[Category: Mitochondrial protein]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| Structural highlights
Disease
CAF17_HUMAN Hypotonia-cerebral atrophy-hyperglycinemia syndrome. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
Function
CAF17_HUMAN Involved in the maturation of mitochondrial 4Fe-4S proteins functioning late in the iron-sulfur cluster assembly pathway.[1]
Publication Abstract from PubMed
This article describes the approach used to solve the structure of human IBA57 in-house by 5-amino-2,4,6-triiodoisophthalic acid (I3C) high-energy-remote single-wavelength anomalous dispersion (SAD) phasing. Multiple orientations of the same triclinic crystal were exploited to acquire sufficient real data multiplicity for phasing. How the collection of an in-house native data set and its joint use with the I3C derivative through a SIRAS approach decreases the data multiplicity needed by almost 50% is described. Furthermore, it is illustrated that there is a clear data-multiplicity threshold value for success and failure in phasing, and how adding further data does not significantly affect substructure solution and model building. To our knowledge, this is the only structure present in the PDB that has been solved in-house by remote SAD phasing in space group P1 using only one crystal. All of the raw data used, derived from the different orientations, have been uploaded to Zenodo in order to enable software developers to improve methods for data processing and structure solution, and for educational purposes.
In-house high-energy-remote SAD phasing using the magic triangle: how to tackle the P1 low symmetry using multiple orientations of the same crystal of human IBA57 to increase the multiplicity.,Gourdoupis S, Nasta V, Ciofi-Baffoni S, Banci L, Calderone V Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):317-324. doi:, 10.1107/S2059798319000214. Epub 2019 Feb 28. PMID:30950402[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ajit Bolar N, Vanlander AV, Wilbrecht C, Van der Aa N, Smet J, De Paepe B, Vandeweyer G, Kooy F, Eyskens F, De Latter E, Delanghe G, Govaert P, Leroy JG, Loeys B, Lill R, Van Laer L, Van Coster R. Mutation of the iron-sulfur cluster assembly gene IBA57 causes severe myopathy and encephalopathy. Hum Mol Genet. 2013 Jul 1;22(13):2590-602. doi: 10.1093/hmg/ddt107. Epub 2013 Mar, 5. PMID:23462291 doi:http://dx.doi.org/10.1093/hmg/ddt107
- ↑ Gourdoupis S, Nasta V, Ciofi-Baffoni S, Banci L, Calderone V. In-house high-energy-remote SAD phasing using the magic triangle: how to tackle the P1 low symmetry using multiple orientations of the same crystal of human IBA57 to increase the multiplicity. Acta Crystallogr D Struct Biol. 2019 Mar 1;75(Pt 3):317-324. doi:, 10.1107/S2059798319000214. Epub 2019 Feb 28. PMID:30950402 doi:http://dx.doi.org/10.1107/S2059798319000214
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