English   español  
Por favor, use este identificador para citar o enlazar a este item: http://hdl.handle.net/10261/110041
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:

RhaU of Rhizobium leguminosarum is a rhamnose mutarotase

AutorRichardson, Jason S.; Carpena, Xavi ; Switala, Jack; Pérez-Luque, Rosa ; Donald, Lynda J.; Loewen, Peter C.; Oresnik, Ivan J.
Fecha de publicaciónabr-2008
EditorAmerican Society for Microbiology
CitaciónJournal of Bacteriology 190(8): 2903-2910 (2008)
ResumenOf the nine genes comprising the L-rhamnose operon of Rhizobium leguminosarum, rhaU has not been assigned a function. The construction of a ΔrhaU strain revealed a growth phenotype that was slower than that of the wild-type strain, although the ultimate cell yields were equivalent. The transport of L-rhamnose into the cell and the rate of its phosphorylation were unaffected by the mutation. RhaU exhibits weak sequence similarity to the formerly hypothetical protein YiiL of Escherichia coli that has recently been characterized as an L-rhamnose mutarotase. To characterize RhaU further, a His-tagged variant of the protein was prepared and subjected to mass spectrometry analysis, confirming the subunit size and demonstrating its dimeric structure. After crystallization, the structure was refined to a 1.6-Å resolution to reveal a dimer in the asymmetric unit with a very similar structure to that of YiiL. Soaking a RhaU crystal with L-rhamnose resulted in the appearance of β-L.-rhamnose in the active site. Copyright © 2008, American Society for Microbiology. All Rights Reserved.
Versión del editorhttp://dx.doi.org/10.1128/JB.01120-07
Identificadoresdoi: 10.1128/JB.01120-07
issn: 0021-9193
Aparece en las colecciones: (IBMB) Artículos
Ficheros en este ítem:
Fichero Descripción Tamaño Formato  
accesoRestringido.pdf15,38 kBAdobe PDFVista previa
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.