English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/12189
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 crystal structure of an eukaryotic iron superoxide dismutase suggests intersubunit cooperation during catalysis

AuthorsMuñoz, Inés G.; Morán, José F. ; Becana Ausejo, Manuel ; Montoya Blanco, Guillermo
Keywordsantioxidants
iron superoxide dismutase
manganese superoxide dismutase
X-ray crystallography
protein–protein interaction
Issue DateFeb-2005
PublisherJohn Wiley & Sons
CitationProtein Science 14(2): 387–394 (2005)
AbstractSuperoxide dismutases (SODs) are a family of metalloenzymes that catalyze the dismutation of superoxide anion radicals into molecular oxygen and hydrogen peroxide. Iron superoxide dismutases (FeSODs) are only expressed in some prokaryotes and plants. A new and highly active FeSOD with an unusual subcellular localization has recently been isolated from the plant Vigna unguiculata (cowpea). This protein functions as a homodimer and, in contrast to the other members of the SOD family, is localized to the cytosol. The crystal structure of the recombinant enzyme has been solved and the model refined to 1.97 Å resolution. The superoxide anion binding site is located in a cleft close to the dimer interface. The coordination geometry of the Fe site is a distorted trigonal bipyramidal arrangement, whose axial ligands are His43 and a solvent molecule, and whose in-plane ligands are His95, Asp195, and His199. A comparison of the structural features of cowpea FeSOD with those of homologous SODs reveals subtle differences in regard to the metal–protein interactions, and confirms the existence of two regions that may control the traffic of substrate and product: one located near the Fe binding site, and another in the dimer interface. The evolutionary conservation of reciprocal interactions of both monomers in neighboring active sites suggests possible subunit cooperation during catalysis.
DescriptionThe definitive version is available at: http://www.proteinscience.org/ http://www3.interscience.wiley.com/journal/121502357/home This article is open access through PubMed Central.
Publisher version (URL)http://dx.doi.org/10.1110/ps.04979505
URIhttp://hdl.handle.net/10261/12189
DOI10.1110/ps.04979505
ISSN0961-8368
Appears in Collections:(EEAD) Artículos
Files in This Item:
File Description SizeFormat 
BecanaM_ProteinSci_2005.pdf245,33 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


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