Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/142034
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Título: | Mechanism of sulfur transfer across protein-protein interfaces: The cysteine desulfurase model system |
Autor: | Fernández, Francisco J. CSIC ORCID; Ardá, Ana CSIC ORCID CVN; López-Estepa, Miguel CSIC; Aranda, Juan; Peña-Soler, Esther CSIC; Garces, Fernando CSIC; Round, Adam; Campos-Olivas, Ramón CSIC ORCID; Bruix, M. CSIC ORCID ; Coll, Miquel CSIC ORCID ; Tuñon, Iñaki; Jiménez-Barbero, Jesús CSIC ORCID; Vega, María Cristina CSIC ORCID | Fecha de publicación: | 2016 | Citación: | ACS Catalysis 6(6): 3975-3984 (2016) | Resumen: | 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. | Versión del editor: | http://doi.org/10.1021/acscatal.6b00360 | URI: | http://hdl.handle.net/10261/142034 | DOI: | 10.1021/acscatal.6b00360 | Identificadores: | doi: 10.1021/acscatal.6b00360 issn: 2155-5435 |
Aparece en las colecciones: | (IQF) Artículos (CIB) Artículos (IBMB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
Fernandez_ACSCatalysis2016_postprint.pdf | 447,52 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
11
checked on 03-abr-2024
WEB OF SCIENCETM
Citations
10
checked on 27-feb-2024
Page view(s)
377
checked on 22-abr-2024
Download(s)
266
checked on 22-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.