Structural/Functional Properties of Human NFU1, an Intermediate [4Fe-4S] Carrier in Human Mitochondrial Iron-Sulfur Cluster Biogenesis

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• 作者：Kai Cai¹ ; Gaohua Liu³ ; Ronnie O. Frederick² ; Rong Xiao³ ; Gaetano T. Montelione³ ; ⁴ ; ^{gtm@rutgers.edu} ; John L. Markley¹ ; ² ; ⁵ ; ^{jmarkley@wisc.edu}
• 关键词：iron-sulfur protein biosynthesis ; NMR spectroscopy ; small-angle X-ray scattering ; Fe-S cluster transfer
• 刊名：Structure
• 出版年：2016
• 出版时间：6 December 2016
• 年：2016
• 卷：24
• 期：12
• 页码：2080-2091
• 全文大小：3071 K
• 卷排序：24

文摘

We determined NMR structures of the isolated N- and C-terminal domains of human NFU1 The domain structures combined with SAXS data yielded a model for full-length apo-NFU1 A holo-NFU1 preparation was shown to be functional in activating apo-aconitase A structural model for holo-NFU1 was derived from combined NMR and SAXS data