Article
Active glutaminase C self-assembles into a supratetrameric oligomer that can be disrupted by an allosteric inhibitor.
The Journal of biological chemistry - 27 Sept 2013
Ferreira Amanda Petrina Scotá, Cassago Alexandre, Gonçalves Kaliandra de Almeida, Dias Marília Meira, Adamoski Douglas, Ascenção Carolline Fernanda Rodrigues, Honorato Rodrigo Vargas, de Oliveira Juliana Ferreira, Ferreira Igor Monteze, Fornezari Camila, Bettini Jefferson, Oliveira Paulo Sérgio Lopes, Paes Leme Adriana Franco, Portugal Rodrigo Villares, Ambrosio Andre Luis Berteli, Dias Sandra Martha Gomes
Abstract excerpt
The phosphate-dependent transition between enzymatically inert dimers into catalytically capable tetramers has long been the accepted mechanism for the glutaminase activation. Here, we demonstrate that activated glutaminase C (GAC) self-assembles into a helical, fiber-like double-stranded oligomer and propose a molecular model consisting of seven tetramer copies per turn per strand interacting via the N-terminal...
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