English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/81579
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:


Regulation of the type IV secretion ATPase TrwD by magnesium: Implications for catalytic mechanism of the secretion ATPase superfamily

AuthorsRipoll-Rozada, Jorge ; Peña, Alejandro ; Rivas, Susana; Moro, Fernando; Cruz, Fernando de la ; Cabezón, Elena ; Arechaga, Ignacio
Issue Date2012
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 287(21): 17408-17414 (2012)
AbstractTrwD, the VirB11 homologue in conjugative plasmid R388, is a member of the large secretion ATPase superfamily, which includes ATPases from bacterial type II and type IV secretion systems, type IV pilus, and archaeal flagellae assembly. Based on structural studies of the VirB11 homologues in Helicobacter pylori and Brucella suis and the archaeal type II secretion ATPase GspE, a unified mechanism for the secretion ATPase superfamily has been proposed. Here, we have found that the ATP turnover of TrwD is down-regulated by physiological concentrations of magnesium. This regulation is exerted by increasing the affinity for ADP, hence delaying product release. Circular dichroism and limited proteolysis analysis indicate that magnesium induces conformational changes in the protein that promote a more rigid, but less active, form of the enzyme. The results shown here provide new insights into the catalytic mechanism of the secretion ATPase superfamily. © 2012 by The American Society for Biochemistry and Molecular Biology, Inc.
Identifiersdoi: 10.1074/jbc.M112.357905
issn: 0021-9258
e-issn: 1083-351X
Appears in Collections:(UBF) Artículos
(IBBTEC) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdf15,38 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.