Title : Comparison of the Response of Bacterial IscU and SufU to Zn2+ and Select Transition-Metal Ions.

Pub. Date : 2018 Mar 16

PMID : 29210568






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 IscU, the central scaffold protein in the bacterial ISC iron-sulfur (Fe-S) cluster biosynthesis system, has long been recognized to bind a Zn2+ ion at its active site. Iron iron-sulfur cluster assembly enzyme Homo sapiens
2 While initially regarded as an artifact, Zn2+ binding has been shown to induce stabilization of the IscU structure that may mimic a state biologically relevant to IscU"s role in Fe-S cluster biosynthesis. Iron iron-sulfur cluster assembly enzyme Homo sapiens
3 While initially regarded as an artifact, Zn2+ binding has been shown to induce stabilization of the IscU structure that may mimic a state biologically relevant to IscU"s role in Fe-S cluster biosynthesis. Iron iron-sulfur cluster assembly enzyme Homo sapiens
4 Monitoring and comparing the conformational behavior and stabilization afforded by different transition metal ions upon IscU and SufU revealed similarities between the two proteins and suggest that metal-dependent conformational transitions may be characteristic of U-type proteins involved in Fe-S cluster biosynthesis. Iron iron-sulfur cluster assembly enzyme Homo sapiens