Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions

Structure of human Fe-S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP-ISD11 interactions

In eukaryotes, sulfur is mobilized for incorporation into multiple biosynthetic pathways by a cysteine desulfurase complex that consists of a catalytic subunit (NFS1), LYR protein (ISD11), and acyl carrier protein (ACP). This NFS1-ISD11-ACP (SDA) complex forms the core of the iron-sulfur (Fe-S) asse...

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Bibliographic Details
Main Authors:	Cory, Seth A. (Author), Van Vranken, Jonathan G. (Author), Brignole, Edward J. (Contributor), Patra, Shachin (Author), Winge, Dennis R. (Author), Drennan, Catherine L. (Contributor), Rutter, Jared (Author), Barondeau, David P. (Author)
Other Authors:	Massachusetts Institute of Technology. Department of Biology (Contributor), Massachusetts Institute of Technology. Department of Chemistry (Contributor)
Format:	Article
Language:	English
Published:	National Academy of Sciences (U.S.), 2018-04-24T14:07:42Z.
Subjects:	Article
Online Access:	Get fulltext

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