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Journal article

Zinc(II) binding on human wild-type ISCU and Met140 variants modulates NFS1 desulfurase activity

Abstract:

Human de novo iron-sulfur (Fe-S) assembly complex consists of cysteine desulfurase NFS1, accessory protein ISD11, acyl carrier protein ACP, scaffold protein ISCU, and allosteric activator frataxin (FXN). FXN binds the NFS1-ISD11-ACP-ISCU complex (SDAU), to activate the desulfurase activity and Fe-S cluster biosynthesis. In the absence of FXN, the NFS1-ISD11-ACP (SDA) complex was reportedly inhibited by binding of recombinant ISCU. Recent studies also reported a substitution at position Met141...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.biochi.2018.07.012

Authors


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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Subgroup:
Structural Genomics Consortium
Martelli, A More by this author
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ORCID:
0000-0002-9600-2347
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
NDM
Subgroup:
Structural Genomics Consortium
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Publisher:
Elsevier Publisher's website
Journal:
Biochimie Journal website
Volume:
152
Pages:
211-218
Publication date:
2018-07-19
Acceptance date:
2018-07-18
DOI:
ISSN:
0300-9084
Pubs id:
pubs:891543
URN:
uri:6caa601d-6772-4175-b472-9304036c27ad
UUID:
uuid:6caa601d-6772-4175-b472-9304036c27ad
Local pid:
pubs:891543

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