Structure of human Fe–S assembly subcomplex reveals unexpected cysteine desulfurase architecture and...
Structure of human Fe–S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP–ISD11 interactions
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United States: National Academy of Sciences
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Language
English
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United States: National Academy of Sciences
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Contents
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) assembly complex and associates with assembly proteins...
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Full title
Structure of human Fe–S assembly subcomplex reveals unexpected cysteine desulfurase architecture and acyl-ACP–ISD11 interactions
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TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5502623
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https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5502623
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ISSN
0027-8424
E-ISSN
1091-6490
DOI
10.1073/pnas.1702849114
