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PDBsum entry 5awf
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Transport protein/protein binding
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PDB id
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5awf
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Contents |
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385 a.a.
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414 a.a.
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243 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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Functional dynamics revealed by the structure of the sufbcd complex, A novel ATP-Binding cassette (abc) protein that serves as a scaffold for iron-Sulfur cluster biogenesis.
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Authors
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K.Hirabayashi,
E.Yuda,
N.Tanaka,
S.Katayama,
K.Iwasaki,
T.Matsumoto,
G.Kurisu,
F.W.Outten,
K.Fukuyama,
Y.Takahashi,
K.Wada.
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Ref.
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J Biol Chem, 2015,
290,
29717-29731.
[DOI no: ]
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PubMed id
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Abstract
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ATP-binding cassette (ABC)-type ATPases are chemomechanical engines involved in
diverse biological pathways. Recent genomic information reveals that ABC ATPase
domains/subunits act not only in ABC transporters and structural maintenance of
chromosome proteins, but also in iron-sulfur (Fe-S) cluster biogenesis. A novel
type of ABC protein, the SufBCD complex, functions in the biosynthesis of
nascent Fe-S clusters in almost all Eubacteria and Archaea, as well as
eukaryotic chloroplasts. In this study, we determined the first crystal
structure of the Escherichia coli SufBCD complex, which exhibits the common
architecture of ABC proteins: two ABC ATPase components (SufC) with
function-specific components (SufB-SufD protomers). Biochemical and
physiological analyses based on this structure provided critical insights into
Fe-S cluster assembly and revealed a dynamic conformational change driven by ABC
ATPase activity. We propose a molecular mechanism for the biogenesis of the Fe-S
cluster in the SufBCD complex.
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