English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/95792
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 | DATACITE
Exportar a otros formatos:

Title

Crystal Structure, SAXS and Kinetic Mechanism of Hyperthermophilic ADP-Dependent Glucokinase from Thermococcus litoralis Reveal a Conserved Mechanism for Catalysis

AuthorsRivas-Pardo, J. A.; Herrera-Morande, A. ; Castro-Fernández, V.; Fernández, Francisco J. ; Vega, María Cristina ; Guixé, V.
KeywordsBiocatalysis
Crystal structure
Enzyme kinetics
Enzyme structure
Enzymes
Glucose
Protein interactions
Issue Date20-Jun-2013
PublisherPublic Library of Science
CitationPLoS ONE 8(6):e66687
Abstract[EN]ADP-dependent glucokinases represent a unique family of kinases that belong to the ribokinase superfamily, being present mainly in hyperthermophilic archaea. For these enzymes there is no agreement about the magnitude of the structural transitions associated with ligand binding and whether they are meaningful to the function of the enzyme. We used the ADP-dependent glucokinase from Termococcus litoralis as a model to investigate the conformational changes observed in X-ray crystallographic structures upon substrate binding and to compare them with those determined in solution in order to understand their interplay with the glucokinase function. Initial velocity studies indicate that catalysis follows a sequential ordered mechanism that correlates with the structural transitions experienced by the enzyme in solution and in the crystal state. The combined data allowed us to resolve the open-closed conformational transition that accounts for the complete reaction cycle and to identify the corresponding clusters of aminoacids residues responsible for it. These results provide molecular bases for a general mechanism conserved across the ADP-dependent kinase family
Publisher version (URL)http://dx.doi.org/10.1371/journal.pone.0066687
URIhttp://hdl.handle.net/10261/95792
DOIhttp://dx.doi.org/10.1371/journal.pone.0066687
ISSN1932-6203
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
PLOS_ONE 2013 Vega, María Cristina.pdf6,04 MBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 


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