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IscU plays a key role in Fe-S cluster biosynthesis as a scaffold for de novo assembly of clusters. Here, we show that six residues around the cluster binding site are functionally essential and cannot be substituted with other amino acids. We also find that the nearby Tyr3 residue is crucial for sulfur-transfer interaction with IscS cysteine desulfurase, presumably because it controls the movement of a flexible catalytic loop.
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This page is a summary of: Identification of IscU residues critical for de novo iron–sulfur cluster assembly, Molecular Microbiology, October 2019, Wiley,
DOI: 10.1111/mmi.14392.
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