English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/151568
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:
Title

The trimer interface in the quaternary structure of the bifunctional prokaryotic FAD synthetase from Corynebacterium ammoniagenes

AuthorsSerrano, Ana; Sebastián, M.; Arilla-Luna, S.; Baquedano, Silvia; Herguedas, Beatriz ; Velázquez-Campoy, Adrián; Martínez-Júlvez, Marta; Medina, Milagros
Issue Date24-Mar-2017
PublisherNature Publishing Group
CitationScientific Reports 7: 404 (2017)
AbstractBifunctional FAD synthetases (FADSs) fold in two independent modules; The C-terminal riboflavin kinase (RFK) catalyzes the RFK activity, while the N-terminal FMN-adenylyltransferase (FMNAT) exhibits the FMNAT activity. The search for macromolecular interfaces in the Corynebacterium ammoniagenes FADS (CaFADS) crystal structure predicts a dimer of trimers organization. Within each trimer, a head-to-tail arrangement causes the RFK and FMNAT catalytic sites of the two neighboring protomers to approach, in agreement with active site residues of one module influencing the activity at the other. We analyze the relevance of the CaFADS head-to-tail macromolecular interfaces to stabilization of assemblies, catalysis and ligand binding. With this aim, we evaluate the effect of point mutations in loop L1c-FlapI, loop L6c, and helix α1c of the RFK module (positions K202, E203,F206, D298, V300, E301 and L304), regions at the macromolecular interface between two protomers within the trimer. Although none of the studied residues is critical in the formation and dissociation of assemblies, residues at L1c-FlapI and helix α1c particularly modulate quaternary architecture, as well as ligand binding and kinetic parameters involved with RFK and FMNAT activities. These data support the influence of transient oligomeric structures on substrate accommodation and catalysis at both CaFADS active sites.
Description13 p.-5 fig.-3 tab.
Publisher version (URL)http://dx.doi.org/10.1038/s41598-017-00402-6
URIhttp://hdl.handle.net/10261/151568
DOI10.1038/s41598-017-00402-6
ISSN2045-2322
E-ISSN2045-2322
Appears in Collections:(IQFR) Artículos
(CIB) Artículos
Files in This Item:
File Description SizeFormat 
Sc. Rep. 2017.pdfArtículo principal2,25 MBAdobe PDFThumbnail
View/Open
Show full item record
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.