English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/35284
COMPARTIR / IMPACTO:
Estadísticas
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:
Título

Quaternary structure of the oxaloacetate decarboxylase membrane complex and mechanistic relationships to pyruvate carboxylases.

AutorBalsera, Mónica ; Buey, Ruben M.; Li, Xiao-Dan
Palabras claveOxaloacetate decarboxylase
SAXS-Small angle x-ray scattering
Membrane protein complex
Homology modelling
Fecha de publicación2011
EditorAmerican Society for Biochemistry and Molecular Biology
CitaciónJournal of Biological Chemistry 286(11): 9457-9467 (2011)
ResumenThe oxaloacetate decarboxylase primary Na pump (OAD) is an essential membrane protein complex that functions in the citrate fermentation pathway of some pathogenic bacteria under anaerobic conditions. OAD contains three different subunits: Oad- , a biotinylated extrinsic protein that catalyzes the -ketodecarboxylation of oxaloacetate; Oad- , a structural bitopic membrane protein whose cytosolic tail (named as Oad- ) binds tightly to Oad- ; and Oad- , a multispan transmembrane -helical protein that constitutes the Na channel. How OAD is organized structurally at the membrane and what the molecular determinants are that lead to an efficient energy coupling mechanism remain elusive. In the present work, we elucidate the stoichiometry of the native complex as well as the low resolution structure of the peripheral components of OAD (Oad- and Oad- ) by small angle x-ray scattering. Our results point to a quaternary assembly similar to the pyruvate carboxylase complex organization. Herein, we propose a model in which the association in pairs of Oad- dimers, mediated by Oad- , results in the acquisition of a functional oligomeric state at the bacterial membrane. New structural insights for the conformational rearrangements associated with the carboxylbiotin transfer reaction within OAD are provided.
Descripción11 páginas, 8 figuras, 1 tabla.
Versión del editorhttp://dx.doi.org/10.1074/jbc.M110.197442
URI10261/35284
DOI10.1074/jbc.M110.197442
ISSN0021-9258
Aparece en las colecciones: (IRNASA) Artículos
(IBMCC) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
Visualizar/Abrir
Mostrar el registro completo
 

Artículos relacionados:


NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.