論文

査読有り
2015年12月

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

JOURNAL OF BIOLOGICAL CHEMISTRY
  • Kei Hirabayashi
  • ,
  • Eiki Yuda
  • ,
  • Naoyuki Tanaka
  • ,
  • Sumie Katayama
  • ,
  • Kenji Iwasaki
  • ,
  • Takashi Matsumoto
  • ,
  • Genji Kurisu
  • ,
  • F. Wayne Outten
  • ,
  • Keiichi Fukuyama
  • ,
  • Yasuhiro Takahashi
  • ,
  • Kei Wada

290
50
開始ページ
29717
終了ページ
29731
記述言語
英語
掲載種別
研究論文(学術雑誌)
DOI
10.1074/jbc.M115.680934
出版者・発行元
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

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.

Web of Science ® 被引用回数 : 23

リンク情報
DOI
https://doi.org/10.1074/jbc.M115.680934
PubMed
https://www.ncbi.nlm.nih.gov/pubmed/26472926
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000366614700005&DestApp=WOS_CPL