5AWG
Crystal structure of Hg-bound SufB-SufC-SufD complex from Escherichia coli
Summary for 5AWG
Entry DOI | 10.2210/pdb5awg/pdb |
Related | 5AWF |
Descriptor | FeS cluster assembly protein SufB, FeS cluster assembly protein SufD, Probable ATP-dependent transporter SufC, ... (4 entities in total) |
Functional Keywords | iron-sulfur clusters, iron-sulfur proteins, abc proteins, abc atpase, transport protein-protein binding complex, transport protein/protein binding |
Biological source | Escherichia coli (strain K12) More |
Total number of polymer chains | 8 |
Total formula weight | 314625.11 |
Authors | Hirabayashi, K.,Wada, K. (deposition date: 2015-07-03, release date: 2015-11-11, Last modification date: 2024-05-29) |
Primary citation | Hirabayashi, K.,Yuda, E.,Tanaka, N.,Katayama, S.,Iwasaki, K.,Matsumoto, T.,Kurisu, G.,Outten, F.W.,Fukuyama, K.,Takahashi, Y.,Wada, K. 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 J.Biol.Chem., 290:29717-29731, 2015 Cited by PubMed Abstract: 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. PubMed: 26472926DOI: 10.1074/jbc.M115.680934 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (4.278 Å) |
Structure validation
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