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The mechanism of the transpersulfuration reaction in a cysteine desulfurase-sulfur acceptor model system

AutorFernández, Francisco J. ; López-Estepa, Miguel ; Peña-Soler, Esther ; Quintana, Juan F. ; Bruix, M. ; Coll, Miquel ; Vega, María Cristina
Fecha de publicación2-jul-2015
Citación1as Jornadas Españolas de Biocatálisis (2015)
ResumenEscherichia coli CsdA cysteine desulfurase (the sulfur donor) and the CsdE sulfur acceptor are involved in biological sulfur trafficking, in iron-sulfur cluster assembly, and tRNA hypermodification [1] in the model bacterium Escherichia coli. CsdA and CsdE form a stable complex through a polar interface. 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 [2,3], the flexibility of the catalytic Cys loops involved has precluded a high resolution view of the active-site geometry and chemical environment responsible to facilitate sulfur transfer. Here, we have used a combination of X-ray crystallography, solution NMR, biophysical 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. A mechanistic view of sulfur transfer across protein-protein interfaces emerges from the structuralanalysis of the CSD system
DescripciónPóster presentado en las 1as Jornadas Españolas de Biocatálisis, celebradas los días 2 y 3 de julio de 2015 en Madrid (España)
Francisco J. Fernández et al.
URIhttp://hdl.handle.net/10261/129665
Aparece en las colecciones: (IQFR) Comunicaciones congresos
(IBMB) Comunicaciones congresos
(CIB) Comunicaciones congresos
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