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., Van Vranken, Jonathan G., Brignole, Edward J., Patra, Shachin, Winge, Dennis R., Drennan, Catherine L., Rutter, Jared, Barondeau, David P.
Other Authors:	Massachusetts Institute of Technology. Department of Biology
Format:	Article
Published:	National Academy of Sciences (U.S.) 2018
Online Access:	http://hdl.handle.net/1721.1/114922 https://orcid.org/0000-0002-4285-6128 https://orcid.org/0000-0001-5486-2755

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