ArticleJournal of molecular biology2009
Molecular dynamism of Fe-S cluster biosynthesis implicated by the structure of the SufC(2)-SufD(2) complex.
Article in Journal of molecular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Intricacies in iron-sulfur cluster function and biogenesis: functional versatility, sulfur sources, and enzyme specificity.RSC chemical biology · 2026Review
- Structural diversity of cysteine desulfurases involved in iron-sulfur cluster biosynthesis.Biophysics and physicobiology · 2022Article
- Fe-S cluster biogenesis by the bacterial Suf pathway.Biochimica et biophysica acta. Molecular cell research · 2020Review
- The unique fold and lability of the [2Fe-2S] clusters of NEET proteins mediate their key functions in health and disease.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Iron-sulfur clusters biogenesis by the SUF machinery: close to the molecular mechanism understanding.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2018Review
- Mapping the key residues of SufB and SufD essential for biosynthesis of iron-sulfur clusters.Scientific reports · 2017Article
- 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.The Journal of biological chemistry · 2015Article
- SufB intein of Mycobacterium tuberculosis as a sensor for oxidative and nitrosative stresses.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Interplay between oxygen and Fe-S cluster biogenesis: insights from the Suf pathway.Biochemistry · 2014Review
- Structural insights of post-translational modification sites in the proteome of Thermus thermophilus.Journal of structural and functional genomics · 2014Article
- Separate FeS scaffold and carrier functions for SufB₂C₂ and SufA during in vitro maturation of [2Fe2S] Fdx.Journal of inorganic biochemistry · 2012Article
- The apicomplexan plastid and its evolution.Cellular and molecular life sciences : CMLS · 2011Review
- SufD and SufC ATPase activity are required for iron acquisition during in vivo Fe-S cluster formation on SufB.Biochemistry · 2010Article
- Iron-sulfur (Fe-S) cluster assembly: the SufBCD complex is a new type of Fe-S scaffold with a flavin redox cofactor.The Journal of biological chemistry · 2010Article
- Building Fe-S proteins: bacterial strategies.Nature reviews. Microbiology · 2010Review
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12 authors.
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Abstract
Maturation of iron-sulfur (Fe-S) proteins is achieved by the SUF machinery in a wide number of eubacteria and archaea, as well as eukaryotic chloroplasts. This machinery is encoded in Escherichia coli by the sufABCDSE operon, where three Suf components, SufB, SufC, and SufD, form a complex and appear to provide an intermediary site for the Fe-S cluster assembly. Here, we report the quaternary structure of the SufC(2)-SufD(2) complex in which SufC is bound to the C-terminal domain of SufD. Comparison with the monomeric structure of SufC revealed conformational change of the active-site residues: SufC becomes competent for ATP binding and hydrolysis upon association with SufD. The two SufC subunits were spatially separated in the SufC(2)-SufD(2) complex, whereas cross-linking experiments in solution have indicated that two SufC molecules associate with each other in the presence of Mg(2+) and ATP. Such dimer formation of SufC may lead to a gross structural change of the SufC(2)-SufD(2) complex. Furthermore, genetic analysis of SufD revealed an essential histidine residue buried inside the dimer interface, suggesting that conformational change may expose this crucial residue. These findings, together with biochemical characterization of the SufB-SufC-SufD complex, have led us to propose a model for the Fe-S cluster biosynthesis in the complex.
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