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Logo of jbcThe Journal of Biological Chemistry
J Biol Chem. 2013 December 20; 288(51): 36201.
PMCID: PMC3868734

Ironing out the Details of How Fe-S Clusters Are Made♦

Escherichia coli SufE Sulfur Transfer Protein Modulates the SufS Cysteine Desulfurase through Allosteric Conformational Dynamics

♦ See referenced article, J. Biol. Chem. 2013, 288, 36189–36200

Iron-sulfur clusters are cofactors that need to be made by dedicated biogenesis proteins. These proteins come together to acquire sulfide and iron ions, use the ions to make clusters, move the Fe-S clusters to the necessary metalloproteins, and keep tabs on the cell's need for Fe-S clusters. To carry out all of these functions, the proteins work closely together, but not much is known about their interactions with one another. In this Paper of the Week, a team led by Laura S. Busenlehner at The University of Alabama and F. Wayne Outten at The University of South Carolina analyzed the bacterial SufS and SufE proteins, which are involved in sulfur mobilization under stress conditions, by using hydrogen/deuterium exchange mass spectrometry. They demonstrated that SufE, which acts as a sulfur acceptor, also triggers a conformational change in the active site of SufS, a cysteine desulfurase. The authors comment, “These results provide a new picture of the SufS-SufE sulfur transferase pathway and suggest a more active role for SufE in promoting the SufS cysteine desulfurase reaction for Fe-S cluster assembly.”

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An abbreviated reaction mechanism for SufS is shown with SufS Lys-226 in green and Cys-364 in purple. SufE Cys-51 is in teal. The pyridoxal 5′-phosphate (PLP) cofactor and substrate cysteine are in black.

Articles from The Journal of Biological Chemistry are provided here courtesy of American Society for Biochemistry and Molecular Biology