5AWF: Crystal Structure Of Sufb-sufc-sufd Complex From Escherichia Coli

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.
PDB ID: 5AWFDownload
MMDB ID: 134081
PDB Deposition Date: 2015/7/3
Updated in MMDB: 2015/11
Experimental Method:
x-ray diffraction
Resolution: 2.96  Å
Source Organism:
Similar Structures:
Biological Unit for 5AWF: tetrameric; determined by author and by software (PISA)
Molecular Components in 5AWF
Label Count Molecule
Proteins (4 molecules)
FES Cluster Assembly Protein Sufb(Gene symbol: sufB)
Molecule annotation
FES Cluster Assembly Protein Sufd(Gene symbol: sufD)
Molecule annotation
Probable Atp-dependent Transporter Sufc(Gene symbol: sufC)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB