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PDBsum entry 5wkp
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Contents |
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396 a.a.
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81 a.a.
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72 a.a.
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118 a.a.
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126 a.a.
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References listed in PDB file
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Key reference
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Title
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Structure and functional dynamics of the mitochondrial fe/s cluster synthesis complex.
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Authors
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M.T.Boniecki,
S.A.Freibert,
U.Mühlenhoff,
R.Lill,
M.Cygler.
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Ref.
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Nat Commun, 2017,
8,
1287.
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PubMed id
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Abstract
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Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many
cellular functions including DNA maintenance, protein translation, and energy
conversion. De novo Fe/S cluster synthesis occurs on the mitochondrial scaffold
protein ISCU and requires cysteine desulfurase NFS1, ferredoxin, frataxin, and
the small factors ISD11 and ACP (acyl carrier protein). Both the mechanism of
Fe/S cluster synthesis and function of ISD11-ACP are poorly understood. Here, we
present crystal structures of three different NFS1-ISD11-ACP complexes with and
without ISCU, and we use SAXS analyses to define the 3D architecture of the
complete mitochondrial Fe/S cluster biosynthetic complex. Our structural and
biochemical studies provide mechanistic insights into Fe/S cluster synthesis at
the catalytic center defined by the active-site Cys of NFS1 and conserved Cys,
Asp, and His residues of ISCU. We assign specific regulatory rather than
catalytic roles to ISD11-ACP that link Fe/S cluster synthesis with mitochondrial
lipid synthesis and cellular energy status.
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