English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/46877
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:


Crystal structure of the hexameric catabolic ornithine transcarbamylase from Lactobacillus hilgardii: structural insights into the oligomeric assembly and metal-binding

AuthorsRivas, Blanca de las ; Fox, Gavin C; Martínez-Ripoll, Martín ; Rodríguez, Héctor ; Muñoz, Rosario ; Mancheño, Jose M.
KeywordsCrystal structure
Metal binding
Oligomeric assembly
Ornithine transcarbamylase
Issue Date23-Oct-2009
CitationJournal of Molecular Biology 393(2): 425–434 (2009)
AbstractCatabolic ornithine transcarbamylase (cOTC; EC catalyzes the formation of ornithine (ORN) and carbamoyl phosphate from citrulline, which constitutes the second step of the degradation of arginine via the arginine deiminase pathway. Here, we report the crystal structure of cOTC from the lactic acid bacteria Lactobacillus hilgardii (Lh-cOTC) refined to 2.1 Å resolution. The structure reveals that Lh-cOTC forms a hexameric assembly, which was also confirmed by gel-filtration chromatography and analytical ultracentrifugation. The homohexamer, with 32 point group symmetry, represents a new oligomeric state within the members of the ornithine transcarbamylase family that are typically homotrimeric or homododecameric. The C-terminal end from each subunit constitutes a key structural element for the stabilization of the hexameric assembly in solution. Additionally, the structure reveals, for the first time in the ornithine transcarbamylase family, a metal-binding site located at the 3-fold molecular symmetry axis of each trimer
Publisher version (URL)http://dx.doi.org/10.1016/j.jmb.2009.08.002
Appears in Collections:(IFI) Artículos
Files in This Item:
File Description SizeFormat 
lactobacillus_hilgardii_Rivas.pdf927,64 kBAdobe PDFThumbnail
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.