2ZU0

Crystal structure of SufC-SufD complex involved in the iron-sulfur cluster biosynthesis

Summary for 2ZU0

• Entry DOI: 10.2210/pdb2zu0/pdb
• Descriptor: Protein sufD, Probable ATP-dependent transporter sufC, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID, ... (4 entities in total)
• Functional Keywords: iron-sulfur cluster, abc-atpase, atp-binding, cytoplasm, nucleotide-binding, transport, biosynthetic protein-protein binding complex, biosynthetic protein/protein binding
• Biological source: Escherichia coli; More
• Cellular location: Cytoplasm: P77499
• Total number of polymer chains: 4
• Total formula weight: 153257.63

Authors

Wada, K. (deposition date: 2008-10-11, release date: 2009-03-10, Last modification date: 2023-11-01)

Primary citation

Wada, K.,Sumi, N.,Nagai, R.,Iwasaki, K.,Sato, T.,Suzuki, K.,Hasegawa, Y.,Kitaoka, S.,Minami, Y.,Outten, F.W.,Takahashi, Y.,Fukuyama, K.
Molecular dynamism of Fe-S cluster biosynthesis implicated by the structure of SufC(2)-SufD(2) complex
J.Mol.Biol., 387:245-258, 2009

PubMed 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.

PubMed: 19361433
DOI: 10.1016/j.jmb.2009.01.054

Experimental method

X-RAY DIFFRACTION (2.2 Å)