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CsdA cysteine desulfurase (the sulfur donor) and the CsdE sulfur acceptor are involved in biological sulfur trafficking and in iron-sulfur cluster assembly in the model bacterium Escherichia coli. CsdA and CsdE form a stable complex through a polar interface that includes CsdA Cys328 and CsdE Cys61, the two residues known to be involved in the sulfur transfer reaction. Although mechanisms for the transfer of a sulfur moiety across protein-protein interfaces have been proposed based on the IscS-IscU and IscS-TusA structures, the flexibility of the catalytic cysteine loops involved has precluded a high resolution view of the active-site geometry and chemical environment for sulfur transfer. Here, we have used a combination of X-ray crystallography, solution NMR and SAXS, isothermal calorimetry, and computational chemistry methods to unravel how CsdA provides a specific recognition platform for CsdE and how their complex organizes a composite functional reaction environment. The X-ray structures of persulfurated (CsdA) and persulfurated (CsdA-CsdE) complexes reveal the crucial roles of the conserved active-site cysteine loop and additional catalytic residues in supporting the transpersulfuration reaction. A mechanistic view of sulfur transfer across protein-protein interfaces that underpins the requirement for the conserved cysteine loop to provide electrostatic stabilization for the in-transfer sulfur atom emerges from the analysis of the persulfurated (CsdA-CsdE) complex structure.BFU2008-02372/BMC, CSD 2006-23, and BFU2011-22588 to M.C., CTQ2012-36253-C03-03 and CTQ2015-66223-C2 to I.T., CTQ2015-64597-C2-1-P to J.J.B., and BFU2010-22266- C02-02 and CTQ2015-66206-C2-2-R to M.C.V. Further support for this work was obtained from the Generalitat Valenciana (ACOMP/2015/239 to I.T.) and from the European Commission FP7 ComplexINC grant (contract no. 279039) to M.C.V.Peer Reviewe

Mechanism of Sulfur Transfer Across Protein–Protein Interfaces: The Cysteine Desulfurase Model System