Journal:Acta Cryst D:S2059798319000214
From Proteopedia
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<b>Molecular Tour</b><br> | <b>Molecular Tour</b><br> | ||
| - | IBA57 is a 325-residue human protein which localizes to the mitochondrion and is part of the iron-sulfur cluster assembly pathway <ref name="Rouault">PMID:25425402</ref>, <ref name="Andreini">PMID:28135316</ref> | + | IBA57 is a 325-residue human protein which localizes to the mitochondrion and is part of the iron-sulfur cluster assembly pathway <ref name="Rouault">PMID:25425402</ref>, <ref name="Andreini">PMID:28135316</ref>. |
| - | The maturation of mitochondrial iron-sulfur proteins requires a complex protein machinery. In the late steps of this machinery, a [2Fe-2S] cluster is converted into a [4Fe-4S] cluster. Human IBA57 protein acts in this step as an iron-sulfur cluster assembly component along with ISCA1 and ISCA2 <ref name="Mikolajczyk">PMID:25347204</ref>, <ref name="Brancaccio">PMID:27989128</ref>, <ref name="Ciofi-Baffoni">PMID:29219157</ref>, <ref name="Gourdoupis">PMID:30269484</ref> | + | The maturation of mitochondrial iron-sulfur proteins requires a complex protein machinery. In the late steps of this machinery, a [2Fe-2S] cluster is converted into a [4Fe-4S] cluster. Human IBA57 protein acts in this step as an iron-sulfur cluster assembly component along with ISCA1 and ISCA2 <ref name="Mikolajczyk">PMID:25347204</ref>, <ref name="Brancaccio">PMID:27989128</ref>, <ref name="Ciofi-Baffoni">PMID:29219157</ref>, <ref name="Gourdoupis">PMID:30269484</ref>. |
The structure of this protein was still unknown and the closest homologue whose structure was determined showed 25% sequence homology only (which made molecular replacement in principle unlikely to be successful). For this reason, experimental phasing was the most likely way to solve it. | The structure of this protein was still unknown and the closest homologue whose structure was determined showed 25% sequence homology only (which made molecular replacement in principle unlikely to be successful). For this reason, experimental phasing was the most likely way to solve it. | ||
This paper (DOI 10.1107/S2059798319000214) describes the approach used to solve in-house the structure of human IBA57 through 5-amino-2,4,6-triiodoisophthalic acid (I3C) high energy remote SAD-phasing. Multiple orientations (each of them corresponding to a different run) of the same P1 (triclinic) crystal have been exploited to acquire sufficient real data multiplicity for successful phasing and thus minimizing the difficulties of merging datasets coming from different crystals. | This paper (DOI 10.1107/S2059798319000214) describes the approach used to solve in-house the structure of human IBA57 through 5-amino-2,4,6-triiodoisophthalic acid (I3C) high energy remote SAD-phasing. Multiple orientations (each of them corresponding to a different run) of the same P1 (triclinic) crystal have been exploited to acquire sufficient real data multiplicity for successful phasing and thus minimizing the difficulties of merging datasets coming from different crystals. | ||
Revision as of 11:50, 13 January 2019
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This page complements a publication in scientific journals and is one of the Proteopedia's Interactive 3D Complement pages. For aditional details please see I3DC.
